{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,2]],"date-time":"2026-10-02T12:01:48Z","timestamp":1790942508023,"version":"4.1.0"},"reference-count":37,"publisher":"Elsevier BV","issue":"2","license":[{"start":{"date-parts":[[2010,9,1]],"date-time":"2010-09-01T00:00:00Z","timestamp":1283299200000},"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":[[2010,9]]},"DOI":"10.1016\/j.jmb.2010.07.036","type":"journal-article","created":{"date-parts":[[2010,7,24]],"date-time":"2010-07-24T10:41:02Z","timestamp":1279968062000},"page":"399-411","source":"Crossref","is-referenced-by-count":11,"title":["Cysteine-to-Serine Mutants Dramatically Reorder the Active Site of Human ABO(H) Blood Group B Glycosyltransferase without Affecting Activity: Structural Insights into Cooperative Substrate Binding"],"prefix":"10.1016","volume":"402","author":[{"given":"Brock","family":"Schuman","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Mattias","family":"Persson","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Roxanne C.","family":"Landry","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Robert","family":"Polakowski","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Joel T.","family":"Weadge","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Nina O.L.","family":"Seto","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Svetlana N.","family":"Borisova","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Monica M.","family":"Palcic","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Stephen V.","family":"Evans","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.jmb.2010.07.036_bb0005","doi-asserted-by":"crossref","first-page":"229","DOI":"10.1038\/345229a0","article-title":"Molecular genetic basis of the histo-blood group ABO system","volume":"345","author":"Yamamoto","year":"1990","journal-title":"Nature"},{"key":"10.1016\/j.jmb.2010.07.036_bb0010","doi-asserted-by":"crossref","first-page":"175","DOI":"10.1111\/j.1423-0410.1993.tb05158.x","article-title":"Molecular genetic analysis of the ABO blood group system: 4. Another type of O allele","volume":"64","author":"Yamamoto","year":"1993","journal-title":"Vox Sang."},{"key":"10.1016\/j.jmb.2010.07.036_bb0015","doi-asserted-by":"crossref","first-page":"525","DOI":"10.1074\/jbc.M410245200","article-title":"Structural basis for the inactivity of human blood group O2 glycosyltransferase","volume":"280","author":"Lee","year":"2005","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jmb.2010.07.036_bb0020","doi-asserted-by":"crossref","first-page":"272","DOI":"10.1016\/0006-291X(68)90380-X","article-title":"An enzymatic basis for blood type B in humans","volume":"32","author":"Kobata","year":"1968","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"10.1016\/j.jmb.2010.07.036_bb0025","first-page":"1132","article-title":"\u00dcber Agglutinationserscheinungen normalen menschlichen Blutes","volume":"14","author":"Landsteiner","year":"1901","journal-title":"Wien. Klin. Wochenschr."},{"key":"10.1016\/j.jmb.2010.07.036_bb0030","doi-asserted-by":"crossref","first-page":"770","DOI":"10.1046\/j.1432-1327.1999.00086.x","article-title":"Donor substrate specificity of recombinant human blood group A, B and hybrid A\/B glycosyltransferases expressed in Escherichia coli","volume":"259","author":"Seto","year":"1999","journal-title":"Eur. J. Biochem."},{"key":"10.1016\/j.jmb.2010.07.036_bb0035","doi-asserted-by":"crossref","first-page":"685","DOI":"10.1038\/nsb832","article-title":"The structural basis for specificity in human ABO(H) blood group biosynthesis","volume":"9","author":"Patenaude","year":"2002","journal-title":"Nat. Struct. Biol."},{"key":"10.1016\/j.jmb.2010.07.036_bb0040","doi-asserted-by":"crossref","first-page":"860","DOI":"10.1107\/S0907444907026479","article-title":"The effect of heavy atoms on the conformation of the active-site polypeptide loop in human ABO(H) blood-group glycosyltransferase B","volume":"63","author":"Letts","year":"2007","journal-title":"Acta Crystallogr., Sect. D: Biol. Crystallogr."},{"key":"10.1016\/j.jmb.2010.07.036_bb0045","doi-asserted-by":"crossref","first-page":"10097","DOI":"10.1074\/jbc.M708669200","article-title":"ABO(H) blood group A and B glycosyltransferases recognize substrate via specific conformational changes","volume":"283","author":"Alfaro","year":"2008","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jmb.2010.07.036_bb0050","doi-asserted-by":"crossref","first-page":"21869","DOI":"10.1074\/jbc.M112343200","article-title":"Crystal structure of beta 1,3-glucuronyltransferase I in complex with active donor substrate UDP-GlcUA","volume":"277","author":"Pedersen","year":"2002","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jmb.2010.07.036_bb0055","doi-asserted-by":"crossref","first-page":"210","DOI":"10.1016\/j.tmrv.2005.02.008","article-title":"The importance of disordered loops in ABO glycosyltransferases","volume":"19","author":"Yazer","year":"2005","journal-title":"Transfus. Med. Rev."},{"key":"10.1016\/j.jmb.2010.07.036_bb0060","doi-asserted-by":"crossref","first-page":"5269","DOI":"10.1093\/emboj\/19.20.5269","article-title":"X-ray crystal structure of rabbit N-acetylglucosaminyltransferase I: catalytic mechanism and a new protein superfamily","volume":"19","author":"Unligil","year":"2000","journal-title":"EMBO J."},{"key":"10.1016\/j.jmb.2010.07.036_bb0065","doi-asserted-by":"crossref","first-page":"166","DOI":"10.1038\/84168","article-title":"Crystal structure of the retaining galactosyltransferase LgtC from Neisseria meningitidis in complex with donor and acceptor sugar analogs","volume":"8","author":"Persson","year":"2001","journal-title":"Nat. Struct. Biol."},{"key":"10.1016\/j.jmb.2010.07.036_bb0070","doi-asserted-by":"crossref","first-page":"28310","DOI":"10.1074\/jbc.M202631200","article-title":"Structural basis of ordered binding of donor and acceptor substrates to the retaining glycosyltransferase, alpha-1,3-galactosyltransferase","volume":"277","author":"Boix","year":"2002","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jmb.2010.07.036_bb0075","doi-asserted-by":"crossref","first-page":"491","DOI":"10.1016\/S0022-2836(02)00020-7","article-title":"Crystal structure of beta1,4-galactosyltransferase complex with UDP-Gal reveals an oligosaccharide acceptor binding site","volume":"318","author":"Ramakrishnan","year":"2002","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.jmb.2010.07.036_bb0080","doi-asserted-by":"crossref","first-page":"53","DOI":"10.1016\/j.tibs.2004.11.005","article-title":"Substrate-induced conformational changes in glycosyltransferases","volume":"30","author":"Qasba","year":"2005","journal-title":"Trends Biochem. Sci."},{"key":"10.1016\/j.jmb.2010.07.036_bb0085","doi-asserted-by":"crossref","first-page":"708","DOI":"10.1016\/j.jmb.2006.03.061","article-title":"Structural basis of carbohydrate transfer activity by human UDP-GalNAc: polypeptide alpha-N-acetylgalactosaminyltransferase (pp-GalNAc-T10)","volume":"359","author":"Kubota","year":"2006","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.jmb.2010.07.036_bb0090","doi-asserted-by":"crossref","first-page":"1270","DOI":"10.1016\/j.jmb.2007.04.012","article-title":"Conformational changes induced by binding UDP-2F-galactose to alpha-1,3 galactosyltransferase\u2014implications for catalysis","volume":"369","author":"Jamaluddin","year":"2007","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.jmb.2010.07.036_bb0095","doi-asserted-by":"crossref","first-page":"37665","DOI":"10.1074\/jbc.M102458200","article-title":"alpha-Lactalbumin (LA) stimulates milk beta-1,4-galactosyltransferase I (beta 4Gal-T1) to transfer glucose from UDP-glucose to N-acetylglucosamine. Crystal structure of beta 4Gal-T1 \u00d7 LA complex with UDP-Glc","volume":"276","author":"Ramakrishnan","year":"2001","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jmb.2010.07.036_bb0100","doi-asserted-by":"crossref","first-page":"587","DOI":"10.1093\/glycob\/cwn043","article-title":"Temperature-dependent cooperativity in donor\u2013acceptor substrate binding to the human blood group glycosyltransferases","volume":"18","author":"Shoemaker","year":"2008","journal-title":"Glycobiology"},{"key":"10.1016\/j.jmb.2010.07.036_bb0105","doi-asserted-by":"crossref","first-page":"718","DOI":"10.1093\/glycob\/cwq019","article-title":"Binding of an acceptor substrate analog enhances the enzymatic activity of human blood Group B galactosyltransferase","volume":"20","author":"Sindhuwinata","year":"2010","journal-title":"Glycobiology"},{"key":"10.1016\/j.jmb.2010.07.036_bb0110","doi-asserted-by":"crossref","first-page":"12403","DOI":"10.1074\/jbc.M212002200","article-title":"A single point mutation reverses the donor specificity of human blood group B-synthesizing galactosyltransferase","volume":"278","author":"Marcus","year":"2003","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jmb.2010.07.036_bb0115","doi-asserted-by":"crossref","unstructured":"Evans, S. V. (1993). SETOR: hardware-lighted three-dimensional solid model representations of macromolecules. J. Mol. Graphics, 11, 134\u2013138, 127\u2013128.","DOI":"10.1016\/0263-7855(93)87009-T"},{"key":"10.1016\/j.jmb.2010.07.036_bb0120","doi-asserted-by":"crossref","first-page":"48608","DOI":"10.1074\/jbc.M108828200","article-title":"Structure of UDP complex of UDP-galactose:beta-galactoside-alpha-1,3-galactosyltransferase at 1.53-\u00c5 resolution reveals a conformational change in the catalytically important C terminus","volume":"276","author":"Boix","year":"2001","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jmb.2010.07.036_bb0125","doi-asserted-by":"crossref","first-page":"2431","DOI":"10.1016\/S0021-9258(17)33605-0","article-title":"Arrangement and conformations of substrates at the active site of pyruvate kinase from model building studies based on magnetic resonance data","volume":"251","author":"Mildvan","year":"1976","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jmb.2010.07.036_bb0130","doi-asserted-by":"crossref","first-page":"4781","DOI":"10.1021\/bi00289a026","article-title":"Conformational states of N-acylglycine dithioesters in solution: resonance Raman studies of isotopically substituted models for enzyme\u2013substrate complexes","volume":"22","author":"Lee","year":"1983","journal-title":"Biochemistry"},{"key":"10.1016\/j.jmb.2010.07.036_bb0135","doi-asserted-by":"crossref","first-page":"13529","DOI":"10.1021\/ja063550r","article-title":"Blood group B galactosyltransferase: insights into substrate binding from NMR experiments","volume":"128","author":"Angulo","year":"2006","journal-title":"J. Am. Chem. Soc."},{"key":"10.1016\/j.jmb.2010.07.036_bb0140","doi-asserted-by":"crossref","first-page":"13512","DOI":"10.1021\/bi035430r","article-title":"Roles of individual enzyme-substrate interactions by alpha-1,3-galactosyltransferase in catalysis and specificity","volume":"42","author":"Zhang","year":"2003","journal-title":"Biochemistry"},{"key":"10.1016\/j.jmb.2010.07.036_bb0145","doi-asserted-by":"crossref","first-page":"1224","DOI":"10.1093\/glycob\/cwp114","article-title":"Comparative study of substrate and product binding to the human ABO(H) blood group glycosyltransferases","volume":"19","author":"Soya","year":"2009","journal-title":"Glycobiology"},{"key":"10.1016\/j.jmb.2010.07.036_bb0150","doi-asserted-by":"crossref","first-page":"323","DOI":"10.1111\/j.1432-1033.1995.323_c.x","article-title":"Expression of a recombinant human glycosyltransferase from a synthetic gene and its utilization for synthesis of the human blood group B trisaccharide","volume":"234","author":"Seto","year":"1995","journal-title":"Eur. J. Biochem."},{"key":"10.1016\/j.jmb.2010.07.036_bb0155","doi-asserted-by":"crossref","first-page":"248","DOI":"10.1016\/0003-2697(76)90527-3","article-title":"A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding","volume":"72","author":"Bradford","year":"1976","journal-title":"Anal. Biochem."},{"key":"10.1016\/j.jmb.2010.07.036_bb0160","doi-asserted-by":"crossref","first-page":"1718","DOI":"10.1107\/S090744499900935X","article-title":"The finer things in X-ray diffraction data collection","volume":"55","author":"Pflugrath","year":"1999","journal-title":"Acta Crystallogr., Sect. D: Biol. Crystallogr."},{"key":"10.1016\/j.jmb.2010.07.036_bb0165","doi-asserted-by":"crossref","first-page":"1022","DOI":"10.1107\/S0021889897006766","article-title":"MOLREP: an automated program for molecular replacement","volume":"30","author":"Vagin","year":"1997","journal-title":"J. Appl. Crystallogr."},{"key":"10.1016\/j.jmb.2010.07.036_bb0170","doi-asserted-by":"crossref","first-page":"240","DOI":"10.1107\/S0907444996012255","article-title":"Refinement of macromolecular structures by the maximum-likelihood method","volume":"53","author":"Murshudov","year":"1997","journal-title":"Acta Crystallogr., Sect. D: Biol. Crystallogr."},{"key":"10.1016\/j.jmb.2010.07.036_bb0175","doi-asserted-by":"crossref","first-page":"760","DOI":"10.1107\/S0907444994003112","article-title":"The CCP4 suite: programs for protein crystallography","volume":"50","year":"1994","journal-title":"Acta Crystallogr., Sect. D: Biol. Crystallogr."},{"key":"10.1016\/j.jmb.2010.07.036_bb0180","doi-asserted-by":"crossref","first-page":"49","DOI":"10.1007\/BF01048331","article-title":"The use of hydrophobic synthetic glycosides as acceptors in glycosyltransferase assays","volume":"5","author":"Palcic","year":"1988","journal-title":"Glycoconjugate J."},{"key":"10.1016\/j.jmb.2010.07.036_bb0185","doi-asserted-by":"crossref","first-page":"161","DOI":"10.1016\/S0008-6215(99)00297-9","article-title":"Enzymatic synthesis of blood group A and B trisaccharide analogues","volume":"324","author":"Seto","year":"2000","journal-title":"Carbohydr. Res."}],"container-title":["Journal of Molecular Biology"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0022283610008016?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0022283610008016?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2021,11,1]],"date-time":"2021-11-01T09:55:47Z","timestamp":1635760547000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0022283610008016"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2010,9]]},"references-count":37,"journal-issue":{"issue":"2","published-print":{"date-parts":[[2010,9]]}},"alternative-id":["S0022283610008016"],"URL":"https:\/\/doi.org\/10.1016\/j.jmb.2010.07.036","relation":{},"ISSN":["0022-2836"],"issn-type":[{"value":"0022-2836","type":"print"}],"subject":[],"published":{"date-parts":[[2010,9]]}}}