{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,4,29]],"date-time":"2026-04-29T08:09:17Z","timestamp":1777450157154,"version":"3.51.4"},"reference-count":60,"publisher":"Portland Press Ltd.","issue":"6","license":[{"start":{"date-parts":[[2019,7,25]],"date-time":"2019-07-25T00:00:00Z","timestamp":1564012800000},"content-version":"vor","delay-in-days":1704,"URL":"http:\/\/creativecommons.org\/licenses\/by\/3.0\/"}],"content-domain":{"domain":["portlandpress.com"],"crossmark-restriction":true},"short-container-title":[],"published-print":{"date-parts":[[2014,12,1]]},"abstract":"<jats:p>The Gram-positive bacterium Staphylococcus pseudintermedius is a leading cause of canine bacterial pyoderma, resulting in worldwide morbidity in dogs. S. pseudintermedius also causes life-threatening human infections. Furthermore, methicillin-resistant S. pseudintermedius is emerging, resembling the human health threat of methicillin-resistant Staphylococcus aureus. Therefore it is increasingly important to characterize targets for intervention strategies to counteract S. pseudintermedius infections. Here we used biophysical methods, mutagenesis, and X-ray crystallography, to define the ligand-binding properties and structure of SitA, an S. pseudintermedius surface lipoprotein. SitA was strongly and specifically stabilized by Mn2+ and Zn2+ ions. Crystal structures of SitA complexed with Mn2+ and Zn2+ revealed a canonical class III solute-binding protein with the metal cation bound in a cavity between N- and C-terminal lobes. Unexpectedly, one crystal contained both apo- and holo-forms of SitA, revealing a large side-chain reorientation of His64, and associated structural differences accompanying ligand binding. Such conformational changes may regulate fruitful engagement of the cognate ABC (ATP-binding cassette) transporter system (SitBC) required for metal uptake. These results provide the first detailed characterization and mechanistic insights for a potential therapeutic target of the major canine pathogen S. pseudintermedius, and also shed light on homologous structures in related staphylococcal pathogens afflicting humans.<\/jats:p>","DOI":"10.1042\/bsr20140088","type":"journal-article","created":{"date-parts":[[2014,10,14]],"date-time":"2014-10-14T04:44:30Z","timestamp":1413261870000},"update-policy":"https:\/\/doi.org\/10.1042\/crossmark_policy","source":"Crossref","is-referenced-by-count":30,"title":["Apo, Zn2+-bound and Mn2+-bound structures reveal ligand-binding properties of SitA from the pathogen\n                    <i>Staphylococcus pseudintermedius<\/i>"],"prefix":"10.1042","volume":"34","author":[{"given":"Francesca","family":"Abate","sequence":"first","affiliation":[{"name":"Novartis Vaccines and Diagnostics srl, Via Fiorentina 1, 53100 Siena, Italy"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Enrico","family":"Malito","sequence":"additional","affiliation":[{"name":"Novartis Vaccines and Diagnostics srl, Via Fiorentina 1, 53100 Siena, Italy"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Roberta","family":"Cozzi","sequence":"additional","affiliation":[{"name":"Novartis Vaccines and Diagnostics srl, Via Fiorentina 1, 53100 Siena, Italy"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Paola","family":"Lo Surdo","sequence":"additional","affiliation":[{"name":"Novartis Vaccines and Diagnostics srl, Via Fiorentina 1, 53100 Siena, Italy"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Domenico","family":"Maione","sequence":"additional","affiliation":[{"name":"Novartis Vaccines and Diagnostics srl, Via Fiorentina 1, 53100 Siena, Italy"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Matthew\u00a0J.","family":"Bottomley","sequence":"additional","affiliation":[{"name":"Novartis Vaccines and Diagnostics srl, Via Fiorentina 1, 53100 Siena, Italy"}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"288","published-online":{"date-parts":[[2014,11,24]]},"reference":[{"key":"2021111618304579100_B1","doi-asserted-by":"publisher","first-page":"8685","DOI":"10.1128\/JB.01150-07","article-title":"Population genetic structure of the Staphylococcus intermedius group: insights into agr diversification and the emergence of methicillin-resistant strains","volume":"189","author":"Bannoehr","year":"2007","journal-title":"J. Bacteriol."},{"key":"2021111618304579100_B2","doi-asserted-by":"publisher","first-page":"490","DOI":"10.1111\/j.1365-3164.2009.00828.x","article-title":"The Staphylococcus intermedius group of bacterial pathogens: species re-classification, pathogenesis and the emergence of meticillin resistance","volume":"20","author":"Fitzgerald","year":"2009","journal-title":"Vet. Dermatol."},{"key":"2021111618304579100_B3","doi-asserted-by":"publisher","first-page":"533","DOI":"10.1136\/vr.158.16.533","article-title":"Survey of the prevalence, diagnosis and treatment of dermatological conditions in small animals in general practice","volume":"158","author":"Hill","year":"2006","journal-title":"Vet. Rec."},{"key":"2021111618304579100_B4","doi-asserted-by":"publisher","first-page":"321","DOI":"10.1093\/jac\/dkh332","article-title":"Pet animals as reservoirs of antimicrobial-resistant bacteria","volume":"54","author":"Guardabassi","year":"2004","journal-title":"J. Antimicrob. Chemother."},{"key":"2021111618304579100_B5","doi-asserted-by":"publisher","first-page":"4609","DOI":"10.1128\/JCM.01308-06","article-title":"First case of Staphylococcus pseudintermedius infection in a human","volume":"44","author":"Van Hoovels","year":"2006","journal-title":"J. Clin. Microbiol."},{"key":"2021111618304579100_B6","doi-asserted-by":"publisher","first-page":"1145","DOI":"10.1093\/jac\/dkq078","article-title":"Clonal spread of methicillin-resistant Staphylococcus pseudintermedius in Europe and North America: an international multicentre study","volume":"65","author":"Perreten","year":"2010","journal-title":"J. Antimicrob. Chemother."},{"key":"2021111618304579100_B7","doi-asserted-by":"publisher","first-page":"1763","DOI":"10.1001\/jama.298.15.1763","article-title":"Invasive methicillin-resistant Staphylococcus aureus infections in the United States","volume":"298","author":"Klevens","year":"2007","journal-title":"J. Am. Med. Assoc."},{"key":"2021111618304579100_B8","doi-asserted-by":"publisher","first-page":"23","DOI":"10.1016\/j.vetmic.2003.09.021","article-title":"Transmission of multiple antimicrobial-resistant Staphylococcus intermedius between dogs affected by deep pyoderma and their owners","volume":"98","author":"Guardabassi","year":"2004","journal-title":"Vet. Microbiol."},{"key":"2021111618304579100_B9","doi-asserted-by":"publisher","first-page":"2363","DOI":"10.1128\/JB.00137-11","article-title":"Complete genome sequence of the canine pathogen Staphylococcus pseudintermedius","volume":"193","author":"Ben Zakour","year":"2011","journal-title":"J. Bacteriol."},{"key":"2021111618304579100_B10","doi-asserted-by":"publisher","first-page":"1783","DOI":"10.1128\/JB.00023-11","article-title":"Complete genome sequence of the veterinary pathogen Staphylococcus pseudintermedius strain HKU10-03, isolated in a case of canine pyoderma","volume":"193","author":"Tse","year":"2011","journal-title":"J. Bacteriol."},{"key":"2021111618304579100_B11","doi-asserted-by":"publisher","first-page":"e1000226","DOI":"10.1371\/journal.ppat.1000226","article-title":"A structural model of the Staphylococcus aureus ClfA-fibrinogen interaction opens new avenues for the design of anti-staphylococcal therapeutics","volume":"4","author":"Ganesh","year":"2008","journal-title":"PLoS Pathog."},{"key":"2021111618304579100_B12","doi-asserted-by":"publisher","first-page":"16942","DOI":"10.1073\/pnas.0606863103","article-title":"Vaccine assembly from surface proteins of Staphylococcus aureus","volume":"103","author":"Stranger-Jones","year":"2006","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"2021111618304579100_B13","doi-asserted-by":"publisher","first-page":"3074","DOI":"10.1128\/IAI.00137-11","article-title":"Genomic and surface proteomic analysis of the canine pathogen Staphylococcus pseudintermedius reveals proteins that mediate adherence to the extracellular matrix","volume":"79","author":"Bannoehr","year":"2011","journal-title":"Infect. Immun."},{"key":"2021111618304579100_B14","doi-asserted-by":"publisher","first-page":"39","DOI":"10.1515\/bc.2011.012","article-title":"A structural and functional analysis of type\u00a0III periplasmic and substrate binding proteins: their role in bacterial siderophore and heme transport","volume":"392","author":"Chu","year":"2011","journal-title":"Biol. Chem."},{"key":"2021111618304579100_B15","doi-asserted-by":"publisher","first-page":"17","DOI":"10.1111\/j.1365-2958.1996.tb02484.x","article-title":"Atomic structure and specificity of bacterial periplasmic receptors for active transport and chemotaxis: variation of common themes","volume":"20","author":"Quiocho","year":"1996","journal-title":"Mol. Microbiol."},{"key":"2021111618304579100_B16","doi-asserted-by":"publisher","first-page":"6757","DOI":"10.1128\/IAI.72.12.6757-6763.2004","article-title":"ATP-binding cassette transporters are targets for the development of antibacterial vaccines and therapies","volume":"72","author":"Garmory","year":"2004","journal-title":"Infect. Immun."},{"key":"2021111618304579100_B17","doi-asserted-by":"publisher","first-page":"1781","DOI":"10.1016\/j.bbamem.2007.07.026","article-title":"Structural biology of bacterial iron uptake","volume":"1778","author":"Krewulak","year":"2008","journal-title":"Biochim. Biophys. Acta"},{"key":"2021111618304579100_B18","doi-asserted-by":"publisher","first-page":"1041","DOI":"10.1093\/infdis\/jis463","article-title":"Staphylococcus aureus FhuD2 is involved in the early phase of staphylococcal dissemination and generates protective immunity in mice","volume":"206","author":"Mishra","year":"2012","journal-title":"J. Infect. Dis."},{"key":"2021111618304579100_B19","doi-asserted-by":"publisher","first-page":"683","DOI":"10.1042\/BJ20121426","article-title":"Structural and functional characterization of the Staphylococcus aureus virulence factor and vaccine candidate FhuD2","volume":"449","author":"Mariotti","year":"2013","journal-title":"Biochem. J."},{"key":"2021111618304579100_B20","doi-asserted-by":"publisher","first-page":"1688","DOI":"10.1093\/infdis\/jis272","article-title":"Staphylococcus aureus manganese transport protein C is a highly conserved cell surface protein that elicits protective immunity against S. aureus and Staphylococcus epidermidis","volume":"205","author":"Anderson","year":"2012","journal-title":"J. Infect. Dis."},{"key":"2021111618304579100_B21","doi-asserted-by":"publisher","first-page":"3429","DOI":"10.1016\/j.jmb.2013.06.033","article-title":"Three-dimensional structure and biophysical characterization of Staphylococcus aureus cell surface antigen-manganese transporter MntC","volume":"425","author":"Gribenko","year":"2013","journal-title":"J. Mol. Biol."},{"key":"2021111618304579100_B22","doi-asserted-by":"publisher","first-page":"1553","DOI":"10.1016\/S0969-2126(98)00153-1","article-title":"The crystal structure of pneumococcal surface antigen PsaA reveals a metal-binding site and a novel structure for a putative ABC-type binding protein","volume":"6","author":"Lawrence","year":"1998","journal-title":"Structure"},{"key":"2021111618304579100_B23","doi-asserted-by":"publisher","first-page":"6184","DOI":"10.1021\/bi900552c","article-title":"Crystal structure and metal binding properties of the lipoprotein MtsA, responsible for iron transport in Streptococcus pyogenes","volume":"48","author":"Sun","year":"2009","journal-title":"Biochemistry"},{"key":"2021111618304579100_B24","doi-asserted-by":"publisher","first-page":"1","DOI":"10.1371\/journal.ppat.1002357","article-title":"A molecular mechanism for bacterial susceptibility to zinc","volume":"7","author":"McDevitt","year":"2011","journal-title":"PLoS Pathogens"},{"key":"2021111618304579100_B25","doi-asserted-by":"publisher","first-page":"187","DOI":"10.1146\/annurev.micro.60.080805.142149","article-title":"Manganese transport and the role of manganese in virulence","volume":"60","author":"Papp-Wallace","year":"2006","journal-title":"Annu. Rev. Microbiol."},{"key":"2021111618304579100_B26","doi-asserted-by":"publisher","first-page":"496","DOI":"10.1016\/S0966-842X(02)02462-9","article-title":"Manganese: elemental defence for a life with oxygen","volume":"10","author":"Horsburgh","year":"2002","journal-title":"Trends Microbiol."},{"key":"2021111618304579100_B27","doi-asserted-by":"publisher","first-page":"1050","DOI":"10.2337\/diacare.14.11.1050","article-title":"Copper, zinc, manganese, and magnesium status and complications of diabetes mellitus","volume":"14","author":"Walter","year":"1991","journal-title":"Diab. Care"},{"key":"2021111618304579100_B28","doi-asserted-by":"publisher","first-page":"81","DOI":"10.1016\/0009-8981(84)90041-X","article-title":"Non-protein bound zinc concentration in human plasma and amniotic fluid measured by ultrafiltration","volume":"144","author":"Bloxam","year":"1984","journal-title":"Clin. Chim. Acta"},{"key":"2021111618304579100_B29","doi-asserted-by":"crossref","first-page":"450","DOI":"10.1093\/clinchem\/36.3.450","article-title":"Manganese content of the cellular components of blood","volume":"36","author":"Milne","year":"1990","journal-title":"Clin. Chem."},{"key":"2021111618304579100_B30","doi-asserted-by":"publisher","first-page":"91","DOI":"10.1007\/978-1-59745-196-3","article-title":"The Polymerase Incomplete Primer Extension (PIPE) method applied to high-throughput cloning and site-directed mutagenesis","volume":"498","author":"Klock","year":"2009","journal-title":"Methods Mol. Biol."},{"key":"2021111618304579100_B31","doi-asserted-by":"publisher","first-page":"291","DOI":"10.1016\/j.jbiotec.2005.08.006","article-title":"Improved solubility of TEV protease by directed evolution","volume":"121","author":"van den Berg","year":"2006","journal-title":"J. Biotechnol."},{"key":"2021111618304579100_B32","doi-asserted-by":"publisher","first-page":"2839","DOI":"10.1096\/fj.09-145631","article-title":"Streptococcus pyogenes SpyCEP: a chemokine-inactivating protease with unique structural and biochemical features","volume":"24","author":"Zingaretti","year":"2010","journal-title":"FASEB J."},{"key":"2021111618304579100_B33","doi-asserted-by":"publisher","first-page":"271","DOI":"10.1107\/S0907444910048675","article-title":"iMOSFLM: a new graphical interface for diffraction-image processing with MOSFLM","volume":"67","author":"Battye","year":"2011","journal-title":"Acta Crystallogr. D Biol. Crystallogr."},{"key":"2021111618304579100_B34","doi-asserted-by":"publisher","first-page":"235","DOI":"10.1107\/S0907444910045749","article-title":"Overview of the CCP4 suite and current developments","volume":"67","author":"Winn","year":"2011","journal-title":"Acta Crystallogr. D Biol. Crystallogr."},{"key":"2021111618304579100_B35","doi-asserted-by":"crossref","first-page":"658","DOI":"10.1107\/S0021889807021206","article-title":"Phaser crystallographic software","volume":"40","author":"McCoy","year":"2007","journal-title":"J. Appl. Crystallogr."},{"key":"2021111618304579100_B36","doi-asserted-by":"publisher","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 Crystallogr D Biol Crystallogr."},{"key":"2021111618304579100_B37","volume-title":"BUSTER version 2.11.4","author":"Bricogne","year":"2011"},{"key":"2021111618304579100_B38","doi-asserted-by":"publisher","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":"2021111618304579100_B39","doi-asserted-by":"publisher","first-page":"12","DOI":"10.1107\/S0907444909042073","article-title":"MolProbity: all-atom structure validation for macromolecular crystallography","volume":"66","author":"Chen","year":"2010","journal-title":"Acta Crystallogr. D Biol. Crystallogr."},{"key":"2021111618304579100_B40","doi-asserted-by":"publisher","first-page":"35","DOI":"10.1038\/nchembio.1382","article-title":"Imperfect coordination chemistry facilitates metal ion release in the Psa permease","volume":"10","author":"Counago","year":"2014","journal-title":"Nat. Chem. Biol."},{"key":"2021111618304579100_B41","doi-asserted-by":"publisher","first-page":"e19510","DOI":"10.1371\/journal.pone.0019510","article-title":"Insight into the interaction of metal ions with TroA from Streptococcus suis","volume":"6","author":"Zheng","year":"2011","journal-title":"PLoS One"},{"key":"2021111618304579100_B42","doi-asserted-by":"publisher","first-page":"970","DOI":"10.1016\/j.jmb.2007.01.041","article-title":"Structural analysis of ABC-family periplasmic zinc binding protein provides new insights into mechanism of ligand uptake and release","volume":"367","author":"Chandra","year":"2007","journal-title":"J. Mol. Biol."},{"key":"2021111618304579100_B43","doi-asserted-by":"publisher","first-page":"1358","DOI":"10.1016\/j.jmb.2007.02.107","article-title":"Crystal structure of the zinc-binding transport protein ZnuA from Escherichia coli reveals an unexpected variation in metal coordination","volume":"368","author":"Li","year":"2007","journal-title":"J. Mol. Biol."},{"key":"2021111618304579100_B44","doi-asserted-by":"publisher","first-page":"13974","DOI":"10.1021\/bi801648r","article-title":"Functional assignment of solute-binding proteins of ABC transporters using a fluorescence-based thermal shift assay","volume":"47","author":"Giuliani","year":"2008","journal-title":"Biochemistry"},{"key":"2021111618304579100_B45","doi-asserted-by":"publisher","first-page":"e1002357","DOI":"10.1371\/journal.ppat.1002357","article-title":"A molecular mechanism for bacterial susceptibility to zinc","volume":"7","author":"McDevitt","year":"2011","journal-title":"PLoS Pathog."},{"key":"2021111618304579100_B46","doi-asserted-by":"publisher","first-page":"15835","DOI":"10.1073\/pnas.0605224103","article-title":"Chemical screening methods to identify ligands that promote protein stability, protein crystallization, and structure determination","volume":"103","author":"Vedadi","year":"2006","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"2021111618304579100_B47","doi-asserted-by":"publisher","first-page":"915","DOI":"10.1107\/S0907444911036225","article-title":"A thermal stability assay can help to estimate the crystallization likelihood of biological samples","volume":"67","author":"Dupeux","year":"2011","journal-title":"Acta Crystallogr. D Biol. Crystallogr."},{"key":"2021111618304579100_B48","doi-asserted-by":"publisher","first-page":"774","DOI":"10.1016\/j.jmb.2007.05.022","article-title":"Inference of macromolecular assemblies from crystalline state","volume":"372","author":"Krissinel","year":"2007","journal-title":"J. Mol. Biol."},{"key":"2021111618304579100_B49","doi-asserted-by":"publisher","first-page":"247","DOI":"10.1080\/0889311X.2010.485616","article-title":"Metals in protein structures: a review of their principal features","volume":"16","author":"Harding","year":"2010","journal-title":"Crystallogr. Rev."},{"key":"2021111618304579100_B50","doi-asserted-by":"publisher","first-page":"1765","DOI":"10.1016\/j.jinorgbio.2008.05.006","article-title":"Data mining of metal ion environments present in protein structures","volume":"102","author":"Zheng","year":"2008","journal-title":"J. Inorg. Biochem."},{"key":"2021111618304579100_B51","doi-asserted-by":"publisher","first-page":"367","DOI":"10.1038\/nature11442","article-title":"Structure of AMP\u2013PNP-bound vitamin B12 transporter BtuCD-F","volume":"490","author":"Korkhov","year":"2012","journal-title":"Nature"},{"key":"2021111618304579100_B52","article-title":"Isothermal titration calorimetry. Current Protocols in Cell Biology\/editorial board, Juan S. Bonifacino et al. Chapter 17, Unit 17, 18","author":"Velazquez-Campoy","year":"2004"},{"key":"2021111618304579100_B53","doi-asserted-by":"publisher","first-page":"961","DOI":"10.1016\/j.jmb.2005.03.006","article-title":"The MntC crystal structure suggests that import of Mn2+ in cyanobacteria is redox controlled","volume":"348","author":"Rukhman","year":"2005","journal-title":"J. Mol. Biol."},{"key":"2021111618304579100_B54","doi-asserted-by":"publisher","first-page":"5814","DOI":"10.1128\/JB.00485-09","article-title":"The laminin-binding protein Lbp from Streptococcus pyogenes is a zinc receptor","volume":"191","author":"Linke","year":"2009","journal-title":"J. Bacteriol."},{"key":"2021111618304579100_B55","doi-asserted-by":"publisher","first-page":"2256","DOI":"10.1107\/S0907444904026460","article-title":"Secondary-structure matching (SSM), a new tool for fast protein structure alignment in three dimensions","volume":"60","author":"Krissinel","year":"2004","journal-title":"Acta Crystallogr. D Biol. Crystallogr."},{"key":"2021111618304579100_B56","doi-asserted-by":"publisher","first-page":"2300","DOI":"10.1128\/JB.184.8.2300-2304.2002","article-title":"The crystal structure of Zn(II)-free Treponema pallidum TroA, a periplasmic metal-binding protein, reveals a closed conformation","volume":"184","author":"Lee","year":"2002","journal-title":"J. Bacteriol."},{"key":"2021111618304579100_B57","doi-asserted-by":"publisher","first-page":"271","DOI":"10.1007\/s00775-007-0320-0","article-title":"Structure and metal binding properties of ZnuA, a periplasmic zinc transporter from Escherichia coli","volume":"13","author":"Yatsunyk","year":"2008","journal-title":"J. Biol. Inorg. Chem."},{"key":"2021111618304579100_B58","doi-asserted-by":"publisher","first-page":"72","DOI":"10.1107\/S0907444905036693","article-title":"Scaling and assessment of data quality","volume":"62","author":"Evans","year":"2006","journal-title":"Acta Crystallogr. D Biol. Crystallogr."},{"key":"2021111618304579100_B59","doi-asserted-by":"publisher","first-page":"3059","DOI":"10.1093\/nar\/gkf436","article-title":"MAFFT: a novel method for rapid multiple sequence alignment based on fast Fourier transform","volume":"30","author":"Katoh","year":"2002","journal-title":"Nucleic Acids Res."},{"key":"2021111618304579100_B60","doi-asserted-by":"publisher","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"}],"container-title":["Bioscience Reports"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/portlandpress.com\/bioscirep\/article-pdf\/doi\/10.1042\/BSR20140088\/477135\/bsr034e154.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"syndication"},{"URL":"https:\/\/portlandpress.com\/bioscirep\/article-pdf\/doi\/10.1042\/BSR20140088\/477135\/bsr034e154.pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2021,11,16]],"date-time":"2021-11-16T13:57:56Z","timestamp":1637071076000},"score":1,"resource":{"primary":{"URL":"https:\/\/portlandpress.com\/bioscirep\/article\/34\/6\/e00154\/56442\/Apo-Zn2-bound-and-Mn2-bound-structures-reveal"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2014,11,24]]},"references-count":60,"journal-issue":{"issue":"6","published-print":{"date-parts":[[2014,12,1]]}},"URL":"https:\/\/doi.org\/10.1042\/bsr20140088","relation":{"is-referenced-by":[{"id-type":"doi","id":"10.1007\/s41207-025-00794-2","asserted-by":"object"}]},"ISSN":["0144-8463","1573-4935"],"issn-type":[{"value":"0144-8463","type":"print"},{"value":"1573-4935","type":"electronic"}],"subject":[],"published":{"date-parts":[[2014,11,24]]},"article-number":"e00154"}}