{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,3]],"date-time":"2026-10-03T12:48:01Z","timestamp":1791031681242,"version":"4.1.0"},"reference-count":56,"publisher":"National Academy of Sciences","issue":"18","content-domain":{"domain":["www.pnas.org"],"crossmark-restriction":true},"short-container-title":["Proc. Natl. Acad. Sci. U.S.A."],"published-print":{"date-parts":[[2011,5,3]]},"abstract":"<jats:p>\n                    Pore-forming toxins (PFTs) are potent cytolytic agents secreted by pathogenic bacteria that protect microbes against the cell-mediated immune system (by targeting phagocytic cells), disrupt epithelial barriers, and liberate materials necessary to sustain growth and colonization. Produced by gram-positive and gram-negative bacteria alike, PFTs are released as water-soluble monomeric or dimeric species, bind specifically to target membranes, and assemble transmembrane channels leading to cell damage and\/or lysis. Structural and biophysical analyses of individual steps in the assembly pathway are essential to fully understanding the dynamic process of channel formation. To work toward this goal, we solved by X-ray diffraction the 2.9-\u212b structure of the 450-kDa heptameric\n                    <jats:italic>Vibrio cholerae<\/jats:italic>\n                    cytolysin (VCC) toxin purified and crystallized in the presence of detergent. This structure, together with our previously determined 2.3-\u212b structure of the VCC water-soluble monomer, reveals in detail the architectural changes that occur within the channel region and accessory lectin domains during pore formation including substantial rearrangements of hydrogen-bonding networks in the pore-forming amphipathic loops. Interestingly, a ring of tryptophan residues forms the narrowest constriction in the transmembrane channel reminiscent of the phenylalanine clamp identified in anthrax protective antigen [Krantz BA, et al. (2005)\n                    <jats:italic>Science<\/jats:italic>\n                    309:777\u2013781]. Our work provides an example of a \u03b2-barrel PFT (\u03b2-PFT) for which soluble and assembled structures are available at high-resolution, providing a template for investigating intermediate steps in assembly.\n                  <\/jats:p>","DOI":"10.1073\/pnas.1017442108","type":"journal-article","created":{"date-parts":[[2011,4,19]],"date-time":"2011-04-19T00:19:39Z","timestamp":1303172379000},"page":"7385-7390","update-policy":"https:\/\/doi.org\/10.1073\/pnas.cm10313","source":"Crossref","is-referenced-by-count":126,"title":["Crystal structure of the\n                    <i>Vibrio cholerae<\/i>\n                    cytolysin heptamer reveals common features among disparate pore-forming toxins"],"prefix":"10.1073","volume":"108","author":[{"given":"Swastik","family":"De","sequence":"first","affiliation":[{"name":"Department of Molecular Biology and Biochemistry, Wesleyan University, 52 Lawn Avenue, Middletown, CT 06459"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Rich","family":"Olson","sequence":"additional","affiliation":[{"name":"Department of Molecular Biology and Biochemistry, Wesleyan University, 52 Lawn Avenue, Middletown, CT 06459"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"341","published-online":{"date-parts":[[2011,4,18]]},"reference":[{"key":"e_1_3_4_1_2","doi-asserted-by":"crossref","first-page":"1293","DOI":"10.1128\/iai.65.4.1293-1298.1997","article-title":"Potent membrane-permeabilizing and cytocidal action of Vibrio cholerae cytolysin on human intestinal cells","volume":"65","author":"Zitzer A","year":"1997","unstructured":"A Zitzer, TM Wassenaar, I Walev, S Bhakdi, Potent membrane-permeabilizing and cytocidal action of Vibrio cholerae cytolysin on human intestinal cells. Infect Immun 65, 1293\u20131298 (1997).","journal-title":"Infect Immun"},{"key":"e_1_3_4_2_2","doi-asserted-by":"crossref","first-page":"285","DOI":"10.1007\/s00430-007-0061-2","article-title":"Pro-inflammatory feedback activation cycle evoked by attack of Vibrio cholerae cytolysin on human neutrophil granulocytes","volume":"197","author":"Valeva A","year":"2008","unstructured":"A Valeva, et al., Pro-inflammatory feedback activation cycle evoked by attack of Vibrio cholerae cytolysin on human neutrophil granulocytes. Med Microbiol Immunol 197, 285\u2013293 (2008).","journal-title":"Med Microbiol Immunol"},{"key":"e_1_3_4_3_2","doi-asserted-by":"crossref","first-page":"e5074","DOI":"10.1371\/journal.pone.0005074","article-title":"The Vibrio cholerae cytolysin promotes chloride secretion from intact human intestinal mucosa","volume":"4","author":"Debellis L","year":"2009","unstructured":"L Debellis, et al., The Vibrio cholerae cytolysin promotes chloride secretion from intact human intestinal mucosa. PLoS One 4, e5074 (2009).","journal-title":"PLoS One"},{"key":"e_1_3_4_4_2","doi-asserted-by":"crossref","first-page":"e7352","DOI":"10.1371\/journal.pone.0007352","article-title":"Successful small intestine colonization of adult mice by Vibrio cholerae requires ketamine anesthesia and accessory toxins","volume":"4","author":"Olivier V","year":"2009","unstructured":"V Olivier, J Queen, KJ Satchell, Successful small intestine colonization of adult mice by Vibrio cholerae requires ketamine anesthesia and accessory toxins. PLoS One 4, e7352 (2009).","journal-title":"PLoS One"},{"key":"e_1_3_4_5_2","doi-asserted-by":"crossref","first-page":"1611","DOI":"10.1016\/j.bbamem.2008.01.026","article-title":"Pore formation: An ancient yet complex form of attack","volume":"1778","author":"Iacovache I","year":"2008","unstructured":"I Iacovache, FG van der Goot, L Pernot, Pore formation: An ancient yet complex form of attack. Biochim Biophys Acta 1778, 1611\u20131623 (2008).","journal-title":"Biochim Biophys Acta"},{"key":"e_1_3_4_6_2","doi-asserted-by":"crossref","first-page":"379","DOI":"10.1110\/ps.0231703","article-title":"Vibrio cholerae cytolysin is composed of an alpha-hemolysin-like core","volume":"12","author":"Olson R","year":"2003","unstructured":"R Olson, E Gouaux, Vibrio cholerae cytolysin is composed of an alpha-hemolysin-like core. Protein Sci 12, 379\u2013383 (2003).","journal-title":"Protein Sci"},{"key":"e_1_3_4_7_2","doi-asserted-by":"crossref","first-page":"134","DOI":"10.1038\/5821","article-title":"Crystal structure of staphylococcal LukF delineates conformational changes accompanying formation of a transmembrane channel","volume":"6","author":"Olson R","year":"1999","unstructured":"R Olson, H Nariya, K Yokota, Y Kamio, E Gouaux, Crystal structure of staphylococcal LukF delineates conformational changes accompanying formation of a transmembrane channel. Nat Struct Biol 6, 134\u2013140 (1999).","journal-title":"Nat Struct Biol"},{"key":"e_1_3_4_8_2","doi-asserted-by":"crossref","first-page":"277","DOI":"10.1016\/S0969-2126(99)80038-0","article-title":"The structure of a Staphylococcus aureus leucocidin component (LukF-PV) reveals the fold of the water-soluble species of a family of transmembrane pore-forming toxins","volume":"7","author":"Pedelacq JD","year":"1999","unstructured":"JD Pedelacq, et al., The structure of a Staphylococcus aureus leucocidin component (LukF-PV) reveals the fold of the water-soluble species of a family of transmembrane pore-forming toxins. Structure 7, 277\u2013287 (1999).","journal-title":"Structure"},{"key":"e_1_3_4_9_2","doi-asserted-by":"crossref","first-page":"41028","DOI":"10.1074\/jbc.M406904200","article-title":"Crystal structure of leucotoxin S component: New insight into the staphylococcal beta-barrel pore-forming toxins","volume":"279","author":"Guillet V","year":"2004","unstructured":"V Guillet, et al., Crystal structure of leucotoxin S component: New insight into the staphylococcal beta-barrel pore-forming toxins. J Biol Chem 279, 41028\u201341037 (2004).","journal-title":"J Biol Chem"},{"key":"e_1_3_4_10_2","doi-asserted-by":"crossref","first-page":"1859","DOI":"10.1126\/science.274.5294.1859","article-title":"Structure of staphylococcal alpha-hemolysin, a heptameric transmembrane pore","volume":"274","author":"Song L","year":"1996","unstructured":"L Song, et al., Structure of staphylococcal alpha-hemolysin, a heptameric transmembrane pore. Science 274, 1859\u20131866 (1996).","journal-title":"Science"},{"key":"e_1_3_4_11_2","doi-asserted-by":"crossref","first-page":"1637","DOI":"10.1016\/S0041-0101(01)00151-9","article-title":"Not as simple as just punching a hole","volume":"39","author":"Fivaz M","year":"2001","unstructured":"M Fivaz, L Abrami, Y Tsitrin, FG van der Goot, Not as simple as just punching a hole. Toxicon 39, 1637\u20131645 (2001).","journal-title":"Toxicon"},{"key":"e_1_3_4_12_2","doi-asserted-by":"crossref","first-page":"243","DOI":"10.1146\/annurev.biochem.75.103004.142728","article-title":"Anthrax toxin: Receptor binding, internalization, pore formation, and translocation","volume":"76","author":"Young JA","year":"2007","unstructured":"JA Young, RJ Collier, Anthrax toxin: Receptor binding, internalization, pore formation, and translocation. Annu Rev Biochem 76, 243\u2013265 (2007).","journal-title":"Annu Rev Biochem"},{"key":"e_1_3_4_13_2","doi-asserted-by":"crossref","first-page":"6199","DOI":"10.1128\/IAI.73.10.6199-6209.2005","article-title":"Cholesterol-dependent cytolysins, a family of versatile pore-forming toxins","volume":"73","author":"Tweten RK","year":"2005","unstructured":"RK Tweten, Cholesterol-dependent cytolysins, a family of versatile pore-forming toxins. Infect Immun 73, 6199\u20136209 (2005).","journal-title":"Infect Immun"},{"key":"e_1_3_4_14_2","doi-asserted-by":"crossref","first-page":"293","DOI":"10.1016\/S0092-8674(00)81660-8","article-title":"The mechanism of membrane insertion for a cholesterol-dependent cytolysin: A novel paradigm for pore-forming toxins","volume":"99","author":"Shatursky O","year":"1999","unstructured":"O Shatursky, et al., The mechanism of membrane insertion for a cholesterol-dependent cytolysin: A novel paradigm for pore-forming toxins. Cell 99, 293\u2013299 (1999).","journal-title":"Cell"},{"key":"e_1_3_4_15_2","doi-asserted-by":"crossref","first-page":"2968","DOI":"10.1128\/iai.64.8.2968-2973.1996","article-title":"Mechanism of membrane damage by El Tor hemolysin of Vibrio cholerae O1","volume":"64","author":"Ikigai H","year":"1996","unstructured":"H Ikigai, A Akatsuka, H Tsujiyama, T Nakae, T Shimamura, Mechanism of membrane damage by El Tor hemolysin of Vibrio cholerae O1. Infect Immun 64, 2968\u20132973 (1996).","journal-title":"Infect Immun"},{"key":"e_1_3_4_16_2","doi-asserted-by":"crossref","first-page":"1375","DOI":"10.1074\/jbc.274.3.1375","article-title":"Oligomerization of Vibrio cholerae cytolysin yields a pentameric pore and has a dual specificity for cholesterol and sphingolipids in the target membrane","volume":"274","author":"Zitzer A","year":"1999","unstructured":"A Zitzer, O Zitzer, S Bhakdi, M Palmer, Oligomerization of Vibrio cholerae cytolysin yields a pentameric pore and has a dual specificity for cholesterol and sphingolipids in the target membrane. J Biol Chem 274, 1375\u20131380 (1999).","journal-title":"J Biol Chem"},{"key":"e_1_3_4_17_2","doi-asserted-by":"crossref","first-page":"997","DOI":"10.1016\/j.jmb.2005.05.045","article-title":"Crystal structure of the Vibrio cholerae cytolysin (VCC) pro-toxin and its assembly into a heptameric transmembrane pore","volume":"350","author":"Olson R","year":"2005","unstructured":"R Olson, E Gouaux, Crystal structure of the Vibrio cholerae cytolysin (VCC) pro-toxin and its assembly into a heptameric transmembrane pore. J Mol Biol 350, 997\u20131016 (2005).","journal-title":"J Mol Biol"},{"key":"e_1_3_4_18_2","doi-asserted-by":"crossref","first-page":"162","DOI":"10.1074\/jbc.272.1.162","article-title":"Carbohydrate-mediated regulation of interaction of Vibrio cholerae hemolysin with erythrocyte and phospholipid vesicle","volume":"272","author":"Saha N","year":"1997","unstructured":"N Saha, KK Banerjee, Carbohydrate-mediated regulation of interaction of Vibrio cholerae hemolysin with erythrocyte and phospholipid vesicle. J Biol Chem 272, 162\u2013167 (1997).","journal-title":"J Biol Chem"},{"key":"e_1_3_4_19_2","doi-asserted-by":"crossref","first-page":"4655","DOI":"10.1128\/iai.64.11.4655-4658.1996","article-title":"In vitro proteolytic processing and activation of the recombinant precursor of El Tor cytolysin\/hemolysin (pro-HlyA) of Vibrio cholerae by soluble hemagglutinin\/protease of V. cholerae, trypsin, and other proteases","volume":"64","author":"Nagamune K","year":"1996","unstructured":"K Nagamune, et al., In vitro proteolytic processing and activation of the recombinant precursor of El Tor cytolysin\/hemolysin (pro-HlyA) of Vibrio cholerae by soluble hemagglutinin\/protease of V. cholerae, trypsin, and other proteases. Infect Immun 64, 4655\u20134658 (1996).","journal-title":"Infect Immun"},{"key":"e_1_3_4_20_2","doi-asserted-by":"crossref","first-page":"21782","DOI":"10.1016\/S0021-9258(19)36680-3","article-title":"Assembly of the oligomeric membrane pore formed by staphylococcal alpha-hemolysin examined by truncation mutagenesis","volume":"267","author":"Walker B","year":"1992","unstructured":"B Walker, M Krishnasastry, L Zorn, H Bayley, Assembly of the oligomeric membrane pore formed by staphylococcal alpha-hemolysin examined by truncation mutagenesis. J Biol Chem 267, 21782\u201321786 (1992).","journal-title":"J Biol Chem"},{"key":"e_1_3_4_21_2","doi-asserted-by":"crossref","first-page":"99","DOI":"10.1016\/1074-5521(95)90282-1","article-title":"An intermediate in the assembly of a pore-forming protein trapped with a genetically-engineered switch","volume":"2","author":"Walker B","year":"1995","unstructured":"B Walker, O Braha, S Cheley, H Bayley, An intermediate in the assembly of a pore-forming protein trapped with a genetically-engineered switch. Chem Biol 2, 99\u2013105 (1995).","journal-title":"Chem Biol"},{"key":"e_1_3_4_22_2","doi-asserted-by":"crossref","first-page":"13298","DOI":"10.1021\/bi971075r","article-title":"Staphylococcal alpha-toxin: Formation of the heptameric pore is partially cooperative and proceeds through multiple intermediate stages","volume":"36","author":"Valeva A","year":"1997","unstructured":"A Valeva, M Palmer, S Bhakdi, Staphylococcal alpha-toxin: Formation of the heptameric pore is partially cooperative and proceeds through multiple intermediate stages. Biochemistry 36, 13298\u201313304 (1997).","journal-title":"Biochemistry"},{"key":"e_1_3_4_23_2","doi-asserted-by":"crossref","first-page":"385","DOI":"10.1038\/nsmb0505-385","article-title":"Prepore for a breakthrough","volume":"12","author":"Bayley H","year":"2005","unstructured":"H Bayley, L Jayasinghe, M Wallace, Prepore for a breakthrough. Nat Struct Mol Biol 12, 385\u2013386 (2005).","journal-title":"Nat Struct Mol Biol"},{"key":"e_1_3_4_24_2","doi-asserted-by":"crossref","first-page":"6","DOI":"10.1016\/j.jsb.2009.07.015","article-title":"Three-dimensional structure of the detergent-solubilized Vibrio cholerae cytolysin (VCC) heptamer by electron cryomicroscopy","volume":"169","author":"He Y","year":"2010","unstructured":"Y He, R Olson, Three-dimensional structure of the detergent-solubilized Vibrio cholerae cytolysin (VCC) heptamer by electron cryomicroscopy. J Struct Biol 169, 6\u201313 (2010).","journal-title":"J Struct Biol"},{"key":"e_1_3_4_25_2","doi-asserted-by":"crossref","first-page":"122","DOI":"10.1016\/S1047-8477(02)00563-4","article-title":"Interaction of the Vibrio cholerae cytolysin (VCC) with cholesterol, some cholesterol esters, and cholesterol derivatives: A TEM study","volume":"139","author":"Harris JR","year":"2002","unstructured":"JR Harris, et al., Interaction of the Vibrio cholerae cytolysin (VCC) with cholesterol, some cholesterol esters, and cholesterol derivatives: A TEM study. J Struct Biol 139, 122\u2013135 (2002).","journal-title":"J Struct Biol"},{"key":"e_1_3_4_26_2","doi-asserted-by":"crossref","first-page":"1665","DOI":"10.1002\/j.1460-2075.1990.tb08287.x","article-title":"Selenomethionyl proteins produced for analysis by multiwavelength anomalous diffraction (MAD): A vehicle for direct determination of three-dimensional structure","volume":"9","author":"Hendrickson WA","year":"1990","unstructured":"WA Hendrickson, JR Horton, DM LeMaster, Selenomethionyl proteins produced for analysis by multiwavelength anomalous diffraction (MAD): A vehicle for direct determination of three-dimensional structure. EMBO J 9, 1665\u20131672 (1990).","journal-title":"EMBO J"},{"key":"e_1_3_4_27_2","doi-asserted-by":"crossref","first-page":"931","DOI":"10.1038\/2804","article-title":"Roll out the barrel","volume":"5","author":"Gouaux E","year":"1998","unstructured":"E Gouaux, Roll out the barrel. Nat Struct Biol 5, 931\u2013932 (1998).","journal-title":"Nat Struct Biol"},{"key":"e_1_3_4_28_2","doi-asserted-by":"crossref","first-page":"457","DOI":"10.1038\/sj.emboj.7600959","article-title":"A rivet model for channel formation by aerolysin-like pore-forming toxins","volume":"25","author":"Iacovache I","year":"2006","unstructured":"I Iacovache, et al., A rivet model for channel formation by aerolysin-like pore-forming toxins. EMBO J 25, 457\u2013466 (2006).","journal-title":"EMBO J"},{"key":"e_1_3_4_29_2","doi-asserted-by":"crossref","first-page":"2455","DOI":"10.1016\/S0006-3495(93)81293-1","article-title":"The pore dimensions of gramicidin A","volume":"65","author":"Smart OS","year":"1993","unstructured":"OS Smart, JM Goodfellow, BA Wallace, The pore dimensions of gramicidin A. Biophys J 65, 2455\u20132460 (1993).","journal-title":"Biophys J"},{"key":"e_1_3_4_30_2","doi-asserted-by":"crossref","first-page":"646","DOI":"10.1111\/j.1432-1033.1996.0646h.x","article-title":"HlyA hemolysin of Vibrio cholerae O1 biotype E1 Tor. Identification of the hemolytic complex and evidence for the formation of anion-selective ion-permeable channels","volume":"240","author":"Menzl K","year":"1996","unstructured":"K Menzl, E Maier, T Chakraborty, R Benz, HlyA hemolysin of Vibrio cholerae O1 biotype E1 Tor. Identification of the hemolytic complex and evidence for the formation of anion-selective ion-permeable channels. Eur J Biochem 240, 646\u2013654 (1996).","journal-title":"Eur J Biochem"},{"key":"e_1_3_4_31_2","doi-asserted-by":"crossref","first-page":"35","DOI":"10.1016\/j.toxicon.2005.09.007","article-title":"A molecular model of the Vibrio cholerae cytolysin transmembrane pore","volume":"47","author":"Pantano S","year":"2006","unstructured":"S Pantano, C Montecucco, A molecular model of the Vibrio cholerae cytolysin transmembrane pore. Toxicon 47, 35\u201340 (2006).","journal-title":"Toxicon"},{"key":"e_1_3_4_32_2","doi-asserted-by":"crossref","first-page":"97","DOI":"10.1007\/s002140050414","article-title":"Ion channels of biological membranes: Prediction of single channel conductance","volume":"101","author":"Ranatunga KM","year":"1999","unstructured":"KM Ranatunga, C Adcock, ID Kerr, GR Smith, MS Sansom, Ion channels of biological membranes: Prediction of single channel conductance. Theor Chem Acc 101, 97\u2013102 (1999).","journal-title":"Theor Chem Acc"},{"key":"e_1_3_4_33_2","doi-asserted-by":"crossref","first-page":"568","DOI":"10.1128\/JB.01049-09","article-title":"The aromatic ring of phenylalanine 334 is essential for oligomerization of Vibrio vulnificus hemolysin","volume":"192","author":"Kashimoto T","year":"2009","unstructured":"T Kashimoto, et al., The aromatic ring of phenylalanine 334 is essential for oligomerization of Vibrio vulnificus hemolysin. J Bacteriol 192, 568\u2013574 (2009).","journal-title":"J Bacteriol"},{"key":"e_1_3_4_34_2","doi-asserted-by":"crossref","first-page":"271","DOI":"10.1016\/j.biochi.2006.12.003","article-title":"Pore formation by Vibrio cholerae cytolysin requires cholesterol in both monolayers of the target membrane","volume":"89","author":"Krasilnikov OV","year":"2007","unstructured":"OV Krasilnikov, et al., Pore formation by Vibrio cholerae cytolysin requires cholesterol in both monolayers of the target membrane. Biochimie 89, 271\u2013277 (2007).","journal-title":"Biochimie"},{"key":"e_1_3_4_35_2","doi-asserted-by":"crossref","first-page":"2195","DOI":"10.1074\/jbc.M510841200","article-title":"Role of the amino latch of staphylococcal alpha-hemolysin in pore formation: A co-operative interaction between the N terminus and position 217","volume":"281","author":"Jayasinghe L","year":"2006","unstructured":"L Jayasinghe, G Miles, H Bayley, Role of the amino latch of staphylococcal alpha-hemolysin in pore formation: A co-operative interaction between the N terminus and position 217. J Biol Chem 281, 2195\u20132204 (2006).","journal-title":"J Biol Chem"},{"key":"e_1_3_4_36_2","doi-asserted-by":"crossref","first-page":"23072","DOI":"10.1074\/jbc.270.39.23072","article-title":"Interactions between residues in staphylococcal alpha-hemolysin revealed by reversion mutagenesis","volume":"270","author":"Panchal RG","year":"1995","unstructured":"RG Panchal, H Bayley, Interactions between residues in staphylococcal alpha-hemolysin revealed by reversion mutagenesis. J Biol Chem 270, 23072\u201323076 (1995).","journal-title":"J Biol Chem"},{"key":"e_1_3_4_37_2","doi-asserted-by":"crossref","first-page":"175","DOI":"10.1083\/jcb.147.1.175","article-title":"Plasma membrane microdomains act as concentration platforms to facilitate intoxication by aerolysin","volume":"147","author":"Abrami L","year":"1999","unstructured":"L Abrami, FG van Der Goot, Plasma membrane microdomains act as concentration platforms to facilitate intoxication by aerolysin. J Cell Biol 147, 175\u2013184 (1999).","journal-title":"J Cell Biol"},{"key":"e_1_3_4_38_2","doi-asserted-by":"crossref","first-page":"321","DOI":"10.1083\/jcb.200211018","article-title":"Anthrax toxin triggers endocytosis of its receptor via a lipid raft-mediated clathrin-dependent process","volume":"160","author":"Abrami L","year":"2003","unstructured":"L Abrami, S Liu, P Cosson, SH Leppla, FG van der Goot, Anthrax toxin triggers endocytosis of its receptor via a lipid raft-mediated clathrin-dependent process. J Cell Biol 160, 321\u2013328 (2003).","journal-title":"J Cell Biol"},{"key":"e_1_3_4_39_2","doi-asserted-by":"crossref","first-page":"4341","DOI":"10.1073\/pnas.0911581107","article-title":"Only two amino acids are essential for cytolytic toxin recognition of cholesterol at the membrane surface","volume":"107","author":"Farrand AJ","year":"2010","unstructured":"AJ Farrand, S LaChapelle, EM Hotze, AE Johnson, RK Tweten, Only two amino acids are essential for cytolytic toxin recognition of cholesterol at the membrane surface. Proc Natl Acad Sci USA 107, 4341\u20134346 (2010).","journal-title":"Proc Natl Acad Sci USA"},{"key":"e_1_3_4_40_2","doi-asserted-by":"crossref","first-page":"1503","DOI":"10.1110\/ps.03561104","article-title":"High resolution crystallographic studies of alpha-hemolysin-phospholipid complexes define heptamer-lipid head group interactions: Implication for understanding protein-lipid interactions","volume":"13","author":"Galdiero S","year":"2004","unstructured":"S Galdiero, E Gouaux, High resolution crystallographic studies of alpha-hemolysin-phospholipid complexes define heptamer-lipid head group interactions: Implication for understanding protein-lipid interactions. Protein Sci 13, 1503\u20131511 (2004).","journal-title":"Protein Sci"},{"key":"e_1_3_4_41_2","doi-asserted-by":"crossref","first-page":"46","DOI":"10.1126\/science.1174621","article-title":"Lipid rafts as a membrane-organizing principle","volume":"327","author":"Lingwood D","year":"2010","unstructured":"D Lingwood, K Simons, Lipid rafts as a membrane-organizing principle. Science 327, 46\u201350 (2010).","journal-title":"Science"},{"key":"e_1_3_4_42_2","doi-asserted-by":"crossref","first-page":"777","DOI":"10.1126\/science.1113380","article-title":"A phenylalanine clamp catalyzes protein translocation through the anthrax toxin pore","volume":"309","author":"Krantz BA","year":"2005","unstructured":"BA Krantz, et al., A phenylalanine clamp catalyzes protein translocation through the anthrax toxin pore. Science 309, 777\u2013781 (2005).","journal-title":"Science"},{"key":"e_1_3_4_43_2","doi-asserted-by":"crossref","first-page":"3453","DOI":"10.1073\/pnas.1000100107","article-title":"Three-dimensional structure of the anthrax toxin pore inserted into lipid nanodiscs and lipid vesicles","volume":"107","author":"Katayama H","year":"2010","unstructured":"H Katayama, et al., Three-dimensional structure of the anthrax toxin pore inserted into lipid nanodiscs and lipid vesicles. 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Proc Natl Acad Sci USA 105, 4346\u20134351 (2008).","journal-title":"Proc Natl Acad Sci USA"},{"key":"e_1_3_4_45_2","doi-asserted-by":"crossref","first-page":"9802","DOI":"10.1073\/pnas.0604000103","article-title":"A loop network within the anthrax toxin pore positions the phenylalanine clamp in an active conformation","volume":"103","author":"Melnyk RA","year":"2006","unstructured":"RA Melnyk, RJ Collier, A loop network within the anthrax toxin pore positions the phenylalanine clamp in an active conformation. Proc Natl Acad Sci USA 103, 9802\u20139807 (2006).","journal-title":"Proc Natl Acad Sci USA"},{"key":"e_1_3_4_46_2","doi-asserted-by":"crossref","first-page":"1030","DOI":"10.1529\/biophysj.104.057406","article-title":"Interactions of peptides with a protein pore","volume":"89","author":"Movileanu L","year":"2005","unstructured":"L Movileanu, JP Schmittschmitt, JM Scholtz, H Bayley, Interactions of peptides with a protein pore. 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Acta Crystallogr D 54, 905\u2013921 (1998).","journal-title":"Acta Crystallogr D"},{"key":"e_1_3_4_55_2","doi-asserted-by":"crossref","first-page":"10037","DOI":"10.1073\/pnas.181342398","article-title":"Electrostatics of nanosystems: Application to microtubules and the ribosome","volume":"98","author":"Baker NA","year":"2001","unstructured":"NA Baker, D Sept, S Joseph, MJ Holst, JA McCammon, Electrostatics of nanosystems: Application to microtubules and the ribosome. Proc Natl Acad Sci USA 98, 10037\u201310041 (2001).","journal-title":"Proc Natl Acad Sci USA"},{"key":"e_1_3_4_56_2","doi-asserted-by":"crossref","first-page":"1605","DOI":"10.1002\/jcc.20084","article-title":"UCSF Chimera\u2014A visualization system for exploratory research and analysis","volume":"25","author":"Pettersen EF","year":"2004","unstructured":"EF Pettersen, et al., UCSF Chimera\u2014A visualization system for exploratory research and analysis. 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