{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,7]],"date-time":"2026-10-07T17:17:38Z","timestamp":1791393458352,"version":"4.3.3"},"reference-count":52,"publisher":"Elsevier BV","issue":"5","license":[{"start":{"date-parts":[[2012,4,1]],"date-time":"2012-04-01T00:00:00Z","timestamp":1333238400000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Journal of Molecular Biology"],"published-print":{"date-parts":[[2012,4]]},"DOI":"10.1016\/j.jmb.2012.01.026","type":"journal-article","created":{"date-parts":[[2012,2,1]],"date-time":"2012-02-01T19:06:49Z","timestamp":1328123209000},"page":"395-405","source":"Crossref","is-referenced-by-count":67,"title":["The Structures of Coiled-Coil Domains from Type III Secretion System Translocators Reveal Homology to Pore-Forming Toxins"],"prefix":"10.1016","volume":"417","author":[{"given":"Michael L.","family":"Barta","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Nicholas E.","family":"Dickenson","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Mrinalini","family":"Patil","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Andrew","family":"Keightley","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Gerald J.","family":"Wyckoff","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"William D.","family":"Picking","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Wendy L.","family":"Picking","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Brian V.","family":"Geisbrecht","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.jmb.2012.01.026_bb0010","doi-asserted-by":"crossref","first-page":"1085","DOI":"10.1111\/j.1365-2958.2008.06237.x","article-title":"The type III secretion system tip complex and translocon","volume":"68","author":"Mueller","year":"2008","journal-title":"Mol. Microbiol."},{"key":"10.1016\/j.jmb.2012.01.026_bb0015","doi-asserted-by":"crossref","first-page":"745","DOI":"10.1515\/bc.2010.079","article-title":"The type III secretion injectisome, a complex nanomachine for intracellular \u201ctoxin\u201d delivery","volume":"391","author":"Cornelis","year":"2010","journal-title":"Biol. Chem."},{"key":"10.1016\/j.jmb.2012.01.026_bb0020","doi-asserted-by":"crossref","first-page":"652","DOI":"10.1046\/j.1365-2958.2001.02200.x","article-title":"Structure and composition of the Shigella flexneri \u201cneedle complex\u201d, a part of its type III secreton","volume":"39","author":"Blocker","year":"2001","journal-title":"Mol. Microbiol."},{"key":"10.1016\/j.jmb.2012.01.026_bb0025","doi-asserted-by":"crossref","first-page":"543","DOI":"10.1110\/ps.051733506","article-title":"Physical characterization of MxiH and PrgI, the needle component of the type III secretion apparatus from Shigella and Salmonella","volume":"15","author":"Darboe","year":"2006","journal-title":"Protein Sci."},{"key":"10.1016\/j.jmb.2012.01.026_bb0030","doi-asserted-by":"crossref","first-page":"1040","DOI":"10.1126\/science.1102610","article-title":"Structural insights into the assembly of the type III secretion needle complex","volume":"306","author":"Marlovits","year":"2004","journal-title":"Science"},{"key":"10.1016\/j.jmb.2012.01.026_bb0035","doi-asserted-by":"crossref","first-page":"1432","DOI":"10.1128\/IAI.73.3.1432-1440.2005","article-title":"IpaD of Shigella flexneri is independently required for regulation of Ipa protein secretion and efficient insertion of IpaB and IpaC into host membranes","volume":"73","author":"Picking","year":"2005","journal-title":"Infect. Immun."},{"key":"10.1016\/j.jmb.2012.01.026_bb0040","doi-asserted-by":"crossref","first-page":"4035","DOI":"10.1074\/jbc.M607945200","article-title":"Self-chaperoning of the type III secretion system needle tip proteins IpaD and BipD","volume":"282","author":"Johnson","year":"2007","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jmb.2012.01.026_bb0045","article-title":"Conformational changes in IpaD from Shigella flexneri upon binding bile salts provide insight into the second step of type III secretion","author":"Dickenson","year":"2010","journal-title":"Biochemistry"},{"key":"10.1016\/j.jmb.2012.01.026_bb0050","doi-asserted-by":"crossref","first-page":"18646","DOI":"10.1074\/jbc.M802799200","article-title":"Deoxycholate interacts with IpaD of Shigella flexneri in inducing the recruitment of IpaB to the type III secretion apparatus needle tip","volume":"283","author":"Stensrud","year":"2008","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jmb.2012.01.026_bb0055","doi-asserted-by":"crossref","first-page":"2626","DOI":"10.1128\/IAI.01599-06","article-title":"Bile salts stimulate recruitment of IpaB to the Shigella flexneri surface, where it colocalizes with IpaD at the tip of the type III secretion needle","volume":"75","author":"Olive","year":"2007","journal-title":"Infect. Immun."},{"key":"10.1016\/j.jmb.2012.01.026_bb0060","doi-asserted-by":"crossref","first-page":"75","DOI":"10.1002\/pro.537","article-title":"The crystal structures of the Salmonella type III secretion system tip protein SipD in complex with deoxycholate and chenodeoxycholate","volume":"20","author":"Chatterjee","year":"2011","journal-title":"Protein Sci."},{"key":"10.1016\/j.jmb.2012.01.026_bb0065","doi-asserted-by":"crossref","first-page":"e1002163","DOI":"10.1371\/journal.ppat.1002163","article-title":"Crystal structure of PrgI\u2013SipD: insight into a secretion competent state of the type three secretion system needle tip and its interaction with host ligands","volume":"7","author":"Lunelli","year":"2011","journal-title":"PLoS Pathog."},{"key":"10.1016\/j.jmb.2012.01.026_bb0070","doi-asserted-by":"crossref","first-page":"2754","DOI":"10.1128\/IAI.00190-09","article-title":"Liposomes recruit IpaC to the Shigella flexneri type III secretion apparatus needle as a final step in secretion induction","volume":"77","author":"Epler","year":"2009","journal-title":"Infect. Immun."},{"key":"10.1016\/j.jmb.2012.01.026_bb0075","doi-asserted-by":"crossref","first-page":"5899","DOI":"10.1128\/jb.175.18.5899-5906.1993","article-title":"Nonpolar mutagenesis of the ipa genes defines IpaB, IpaC, and IpaD as effectors of Shigella flexneri entry into epithelial cells","volume":"175","author":"M\u00e9nard","year":"1993","journal-title":"J. Bacteriol."},{"key":"10.1016\/j.jmb.2012.01.026_bb0080","doi-asserted-by":"crossref","first-page":"12529","DOI":"10.1073\/pnas.0602689103","article-title":"Molecular model of a type III secretion system needle: implications for host-cell sensing","volume":"103","author":"Deane","year":"2006","journal-title":"Proc. Natl Acad. Sci. USA"},{"key":"10.1016\/j.jmb.2012.01.026_bb0085","doi-asserted-by":"crossref","first-page":"322","DOI":"10.1016\/j.jmb.2006.03.028","article-title":"Solution structure of monomeric BsaL, the type III secretion needle protein of Burkholderia pseudomallei","volume":"359","author":"Zhang","year":"2006","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.jmb.2012.01.026_bb0090","doi-asserted-by":"crossref","first-page":"1304","DOI":"10.1016\/j.jmb.2007.06.034","article-title":"Differences in the electrostatic surfaces of the type III secretion needle proteins PrgI, BsaL, and MxiH","volume":"371","author":"Wang","year":"2007","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.jmb.2012.01.026_bb0095","doi-asserted-by":"crossref","first-page":"819","DOI":"10.1016\/j.jmb.2007.12.067","article-title":"Structural characterization of the Yersinia pestis type III secretion system needle protein YscF in complex with its heterodimeric chaperone YscE\/YscG","volume":"377","author":"Sun","year":"2008","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.jmb.2012.01.026_bb0100","doi-asserted-by":"crossref","first-page":"7803","DOI":"10.1073\/pnas.0610098104","article-title":"Structure of the heterotrimeric complex that regulates type III secretion needle formation","volume":"104","author":"Quinaud","year":"2007","journal-title":"Proc. Natl Acad. Sci. USA"},{"key":"10.1016\/j.jmb.2012.01.026_bb0105","first-page":"301","article-title":"The structure of Yersinia pestis V-antigen, an essential virulence factor and mediator of immunity against plague","volume":"12","author":"Derewenda","year":"2004","journal-title":"Structure"},{"key":"10.1016\/j.jmb.2012.01.026_bb0110","doi-asserted-by":"crossref","first-page":"540","DOI":"10.1038\/nrmicro1662","article-title":"Clinical trials of Shigella vaccines: two steps forward and one step back on a long, hard road","volume":"5","author":"Levine","year":"2007","journal-title":"Nat. Rev., Microbiol."},{"key":"10.1016\/j.jmb.2012.01.026_bb0115","doi-asserted-by":"crossref","first-page":"1715","DOI":"10.1046\/j.1365-2958.2002.03124.x","article-title":"A Salmonella SipB-derived polypeptide blocks the \u201ctrigger\u201d mechanism of bacterial entry into eukaryotic cells","volume":"45","author":"Hayward","year":"2002","journal-title":"Mol. Microbiol."},{"key":"10.1016\/j.jmb.2012.01.026_bb0120","doi-asserted-by":"crossref","first-page":"1309","DOI":"10.1046\/j.1365-2958.2002.02958.x","article-title":"Topology of the Salmonella invasion protein SipB in a model bilayer","volume":"44","author":"McGhie","year":"2002","journal-title":"Mol. Microbiol."},{"key":"10.1016\/j.jmb.2012.01.026_bb0125","doi-asserted-by":"crossref","first-page":"425","DOI":"10.1046\/j.1365-2958.2003.03559.x","article-title":"The purified Shigella IpaB and Salmonella SipB translocators share biochemical properties and membrane topology","volume":"49","author":"Hume","year":"2003","journal-title":"Mol. Microbiol."},{"key":"10.1016\/j.jmb.2012.01.026_bb0130","doi-asserted-by":"crossref","first-page":"515","DOI":"10.1016\/0092-8674(94)90260-7","article-title":"Extracellular association and cytoplasmic partitioning of the IpaB and IpaC invasins of S. flexneri","volume":"79","author":"M\u00e9nard","year":"1994","journal-title":"Cell"},{"key":"10.1016\/j.jmb.2012.01.026_bb0135","doi-asserted-by":"crossref","first-page":"3965","DOI":"10.1128\/jb.177.14.3965-3971.1995","article-title":"Homologs of the Shigella IpaB and IpaC invasins are required for Salmonella typhimurium entry into cultured epithelial cells","volume":"177","author":"Kaniga","year":"1995","journal-title":"J. Bacteriol."},{"key":"10.1016\/j.jmb.2012.01.026_bb0140","doi-asserted-by":"crossref","first-page":"345","DOI":"10.1016\/0882-4010(88)90062-9","article-title":"Nucleotide sequence of the invasion plasmid antigen B and C genes (ipaB and ipaC) of Shigella flexneri","volume":"4","author":"Baudry","year":"1988","journal-title":"Microb. Pathog."},{"key":"10.1016\/j.jmb.2012.01.026_bb0145","series-title":"Protein Sequencing and Identification Using Tandem Mass Spectrometry","author":"Kinter","year":"2000"},{"key":"10.1016\/j.jmb.2012.01.026_bb0150","doi-asserted-by":"crossref","first-page":"307","DOI":"10.1016\/S0076-6879(97)76066-X","article-title":"Processing of X-ray diffraction data collected in oscillation mode","volume":"276","author":"Otwinowski","year":"1997","journal-title":"Methods Enzymol."},{"key":"10.1016\/j.jmb.2012.01.026_bb0155","doi-asserted-by":"crossref","first-page":"213","DOI":"10.1107\/S0907444909052925","article-title":"PHENIX: a comprehensive python-based system for macromolecular structure solution","volume":"66","author":"Adams","year":"2010","journal-title":"Acta Cryst. D Biol. Crystallogr."},{"key":"10.1016\/j.jmb.2012.01.026_bb0160","doi-asserted-by":"crossref","first-page":"2126","DOI":"10.1107\/S0907444904019158","article-title":"Coot: model-building tools for molecular graphics","volume":"60","author":"Emsley","year":"2004","journal-title":"Acta Crystallogr. D Biol. Crystallogr."},{"key":"10.1016\/j.jmb.2012.01.026_bb0165","doi-asserted-by":"crossref","first-page":"486","DOI":"10.1107\/S0907444910007493","article-title":"Features and development of Coot","volume":"66","author":"Emsley","year":"2010","journal-title":"Acta Crystallogr. D Biol. Crystallogr."},{"key":"10.1016\/j.jmb.2012.01.026_bb0170","author":"DeLano"},{"key":"10.1016\/j.jmb.2012.01.026_bb0175","doi-asserted-by":"crossref","first-page":"1269","DOI":"10.1128\/JB.183.4.1269-1276.2001","article-title":"Structure\u2013function analysis of the Shigella virulence factor IpaB","volume":"183","author":"Guichon","year":"2001","journal-title":"J. Bacteriol."},{"key":"10.1016\/j.jmb.2012.01.026_bb0180","doi-asserted-by":"crossref","first-page":"8259","DOI":"10.1073\/pnas.92.18.8259","article-title":"Predicting coiled coils by use of pairwise residue correlations","volume":"92","author":"Berger","year":"1995","journal-title":"Proc. Natl Acad. Sci. USA"},{"key":"10.1016\/j.jmb.2012.01.026_bb0185","doi-asserted-by":"crossref","first-page":"3370","DOI":"10.1093\/nar\/gkg571","article-title":"LGA: a method for finding 3D similarities in protein structures","volume":"31","author":"Zemla","year":"2003","journal-title":"Nucleic Acids Res."},{"key":"10.1016\/j.jmb.2012.01.026_bb0190","doi-asserted-by":"crossref","first-page":"4673","DOI":"10.1093\/nar\/22.22.4673","article-title":"CLUSTALW: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice","volume":"22","author":"Thompson","year":"1994","journal-title":"Nucleic Acids Res."},{"key":"10.1016\/j.jmb.2012.01.026_bb0195","doi-asserted-by":"crossref","first-page":"305","DOI":"10.1093\/bioinformatics\/15.4.305","article-title":"ESPript: analysis of multiple sequence alignments in PostScript","volume":"15","author":"Gouet","year":"1999","journal-title":"Bioinformatics"},{"key":"10.1016\/j.jmb.2012.01.026_bb0200","doi-asserted-by":"crossref","first-page":"704","DOI":"10.1110\/ps.062645007","article-title":"Conformational stability and differential structural analysis of LcrV, PcrV, BipD, and SipD from type III secretion systems","volume":"16","author":"Espina","year":"2007","journal-title":"Protein Sci."},{"key":"10.1016\/j.jmb.2012.01.026_bb0205","doi-asserted-by":"crossref","first-page":"905","DOI":"10.1046\/j.1365-2958.2002.03083.x","article-title":"Coiled-coil proteins associated with type III secretion systems: a versatile domain revisited","volume":"45","author":"Delahay","year":"2002","journal-title":"Mol. Microbiol."},{"key":"10.1016\/j.jmb.2012.01.026_bb0210","doi-asserted-by":"crossref","first-page":"2792","DOI":"10.1074\/jbc.M208383200","article-title":"Structure\u2013function analysis of invasion plasmid antigen C (IpaC) from Shigella flexneri","volume":"278","author":"Kueltzo","year":"2003","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jmb.2012.01.026_bb0215","doi-asserted-by":"crossref","first-page":"W545","DOI":"10.1093\/nar\/gkq366","article-title":"Dali server: conservation mapping in 3D","volume":"38","author":"Holm","year":"2010","journal-title":"Nucleic Acids Res."},{"key":"10.1016\/j.jmb.2012.01.026_bb0220","doi-asserted-by":"crossref","first-page":"1053","DOI":"10.1016\/S1097-2765(01)00396-3","article-title":"Crystal structure of colicin E3: implications for cell entry and ribosome inactivation","volume":"8","author":"Soelaiman","year":"2001","journal-title":"Mol. Cell"},{"key":"10.1016\/j.jmb.2012.01.026_bb0225","doi-asserted-by":"crossref","first-page":"461","DOI":"10.1038\/385461a0","article-title":"Crystal structure of colicin Ia","volume":"385","author":"Wiener","year":"1997","journal-title":"Nature"},{"key":"10.1016\/j.jmb.2012.01.026_bb0230","doi-asserted-by":"crossref","first-page":"843","DOI":"10.1038\/nrmicro2454","article-title":"Swimming against the tide: progress and challenges in our understanding of colicin translocation","volume":"8","author":"Kleanthous","year":"2010","journal-title":"Nat. Rev., Microbiol."},{"key":"10.1016\/j.jmb.2012.01.026_bb0235","doi-asserted-by":"crossref","first-page":"239","DOI":"10.1016\/j.bbamem.2004.07.001","article-title":"On the role of lipid in colicin pore formation","volume":"1666","author":"Zakharov","year":"2004","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.jmb.2012.01.026_bb0240","doi-asserted-by":"crossref","first-page":"711","DOI":"10.1111\/j.1365-2958.2003.03884.x","article-title":"Crystal structure of the cytotoxic bacterial protein colicin B at 2.5\u00a0\u00c5 resolution","volume":"51","author":"Hilsenbeck","year":"2004","journal-title":"Mol. Microbiol."},{"key":"10.1016\/j.jmb.2012.01.026_bb0245","doi-asserted-by":"crossref","first-page":"399","DOI":"10.1016\/S0300-9084(02)01455-4","article-title":"Mechanisms of colicin binding and transport through outer membrane porins","volume":"84","author":"Cao","year":"2002","journal-title":"Biochimie"},{"key":"10.1016\/j.jmb.2012.01.026_bb0250","doi-asserted-by":"crossref","first-page":"597","DOI":"10.1038\/nsb0994-597","article-title":"The domain structure of the ion channel-forming protein colicin Ia","volume":"1","author":"Ghosh","year":"1994","journal-title":"Nat. Struct. Biol."},{"key":"10.1016\/j.jmb.2012.01.026_bb0255","doi-asserted-by":"crossref","first-page":"W284","DOI":"10.1093\/nar\/gki418","article-title":"FFAS03: a server for profile\u2013profile sequence alignments","volume":"33","author":"Jaroszewski","year":"2005","journal-title":"Nucleic Acids Res."},{"key":"10.1016\/j.jmb.2012.01.026_bb0260","doi-asserted-by":"crossref","first-page":"134","DOI":"10.1128\/CMR.00032-07","article-title":"Molecular pathogenesis of Shigella spp.: controlling host cell signaling, invasion, and death by type III secretion","volume":"21","author":"Schroeder","year":"2008","journal-title":"Clin. Microbiol. Rev."},{"key":"10.1016\/j.jmb.2012.01.026_bb0265","doi-asserted-by":"crossref","first-page":"4391","DOI":"10.1128\/IAI.00440-06","article-title":"IpaD localizes to the tip of the type III secretion system needle of Shigella flexneri","volume":"74","author":"Espina","year":"2006","journal-title":"Infect. Immun."}],"container-title":["Journal of Molecular Biology"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0022283612000800?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0022283612000800?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2018,11,26]],"date-time":"2018-11-26T17:52:38Z","timestamp":1543254758000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0022283612000800"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2012,4]]},"references-count":52,"journal-issue":{"issue":"5","published-print":{"date-parts":[[2012,4]]}},"alternative-id":["S0022283612000800"],"URL":"https:\/\/doi.org\/10.1016\/j.jmb.2012.01.026","relation":{},"ISSN":["0022-2836"],"issn-type":[{"value":"0022-2836","type":"print"}],"subject":[],"published":{"date-parts":[[2012,4]]}}}