{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,3,30]],"date-time":"2026-03-30T10:13:48Z","timestamp":1774865628314,"version":"3.50.1"},"reference-count":50,"publisher":"Elsevier BV","issue":"11","license":[{"start":{"date-parts":[[2000,11,1]],"date-time":"2000-11-01T00:00:00Z","timestamp":973036800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2013,7,17]],"date-time":"2013-07-17T00:00:00Z","timestamp":1374019200000},"content-version":"vor","delay-in-days":4641,"URL":"https:\/\/www.elsevier.com\/open-access\/userlicense\/1.0\/"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Structure"],"published-print":{"date-parts":[[2000,11]]},"DOI":"10.1016\/s0969-2126(00)00526-8","type":"journal-article","created":{"date-parts":[[2002,7,25]],"date-time":"2002-07-25T14:41:58Z","timestamp":1027608118000},"page":"1167-1178","source":"Crossref","is-referenced-by-count":78,"title":["Crystal Structure of the Escherichia coli Peptide Methionine Sulphoxide Reductase at 1.9 \u00c5 Resolution"],"prefix":"10.1016","volume":"8","author":[{"given":"Fr\u00e9d\u00e9rique","family":"T\u00eate-Favier","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"David","family":"Cobessi","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Sandrine","family":"Boschi-Muller","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Sa\u0131\u0308d","family":"Azza","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Guy","family":"Branlant","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Andr\u00e9","family":"Aubry","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"78","reference":[{"key":"10.1016\/S0969-2126(00)00526-8_BIB1","doi-asserted-by":"crossref","first-page":"93","DOI":"10.1016\/0891-5849(94)00158-G","article-title":"Oxidation of methionyl residues in proteins","volume":"18","author":"Vogt","year":"1995","journal-title":"Free Radic. Biol. Med."},{"key":"10.1016\/S0969-2126(00)00526-8_BIB2","doi-asserted-by":"crossref","first-page":"271","DOI":"10.1016\/0003-9861(83)90592-1","article-title":"Biochemistry and physiological role of methionine sulfoxide residues in proteins","volume":"223","author":"Brot","year":"1983","journal-title":"Arch. Biochem. Biophys."},{"key":"10.1016\/S0969-2126(00)00526-8_BIB3","doi-asserted-by":"crossref","first-page":"2155","DOI":"10.1073\/pnas.78.4.2155","article-title":"Enzymatic reduction of protein-bound methionine sulfoxide","volume":"78","author":"Brot","year":"1981","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/S0969-2126(00)00526-8_BIB4","doi-asserted-by":"crossref","first-page":"1549","DOI":"10.1016\/S0021-9258(19)49570-7","article-title":"Cloning, sequencing, and expression of the Escherichia coli peptide methionine sulfoxide reductase gene","volume":"267","author":"Rahman","year":"1992","journal-title":"J. Biol. Chem."},{"key":"10.1016\/S0969-2126(00)00526-8_BIB5","doi-asserted-by":"crossref","first-page":"7483","DOI":"10.1073\/pnas.78.12.7483","article-title":"Enzymatic reduction of oxidized \u03b1-1-proteinase inhibitor restores biological activity","volume":"78","author":"Abrams","year":"1981","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/S0969-2126(00)00526-8_BIB6","first-page":"301","article-title":"Human methionine sulfoxide-peptide reductase, an enzyme capable of reactivating oxidized alpha-1-proteinase inhibitor in vivo","volume":"127","author":"Carp","year":"1983","journal-title":"Am. Rev. Respir. Dis"},{"key":"10.1016\/S0969-2126(00)00526-8_BIB7","doi-asserted-by":"crossref","first-page":"196","DOI":"10.1016\/S0014-5793(98)00908-9","article-title":"Enzymatic repair of oxidative damage to human apolipoprotein A-I","volume":"433","author":"Sigalov","year":"1998","journal-title":"FEBS Letters"},{"key":"10.1016\/S0969-2126(00)00526-8_BIB8","doi-asserted-by":"crossref","first-page":"502","DOI":"10.1128\/jb.177.3.502-507.1995","article-title":"Escherichia coli peptide methionine sulfoxide reductase gene","volume":"177","author":"Moskovitz","year":"1995","journal-title":"J. Bacteriol."},{"key":"10.1016\/S0969-2126(00)00526-8_BIB9","doi-asserted-by":"crossref","first-page":"9585","DOI":"10.1073\/pnas.94.18.9585","article-title":"The yeast peptide-methionine sulfoxide reductase functions as an antioxidant in vivo","volume":"94","author":"Moskovitz","year":"1997","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/S0969-2126(00)00526-8_BIB10","doi-asserted-by":"crossref","first-page":"1660","DOI":"10.1046\/j.1471-4159.1999.0731660.x","article-title":"Decrease in peptide methionine sulfoxide reductase in Alzheimer's disease brain","volume":"73","author":"Gabbita","year":"1999","journal-title":"J. Neurochem."},{"key":"10.1016\/S0969-2126(00)00526-8_BIB11","doi-asserted-by":"crossref","first-page":"323","DOI":"10.1016\/S0047-6374(98)00152-3","article-title":"Methionine residues may protect proteins from critical oxidative damage","volume":"107","author":"Levine","year":"1999","journal-title":"Mech. Ageing Dev."},{"key":"10.1016\/S0969-2126(00)00526-8_BIB12","first-page":"887","article-title":"The minimal gene set member msrA is a virulence determinant of the plant pathogen Erwinia chrysanthemi","volume":"96","author":"El Hassouni","year":"1999","journal-title":"Biochemistry"},{"key":"10.1016\/S0969-2126(00)00526-8_BIB13","doi-asserted-by":"crossref","first-page":"251","DOI":"10.1016\/0161-5890(92)90106-8","article-title":"Activation of the fifth component of human complement C5, without cleavage, by methionine oxidizing agents","volume":"29","author":"Vogt","year":"1992","journal-title":"Mol. Immunol."},{"key":"10.1016\/S0969-2126(00)00526-8_BIB14","doi-asserted-by":"crossref","first-page":"105","DOI":"10.1021\/bi981295k","article-title":"Repair of oxidized calmodulin by methionine sulfoxide reductase restores ability to activate the plasma membrane Ca-ATPase","volume":"38","author":"Sun","year":"1999","journal-title":"Biochemistry"},{"key":"10.1016\/S0969-2126(00)00526-8_BIB15","doi-asserted-by":"crossref","first-page":"9932","DOI":"10.1073\/pnas.94.18.9932","article-title":"Modulation of potassium channel function by methionine oxidation and reduction","volume":"94","author":"Ciorba","year":"1997","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/S0969-2126(00)00526-8_BIB16","doi-asserted-by":"crossref","first-page":"7985","DOI":"10.1073\/pnas.93.15.7985","article-title":"Peptide methionine sulfoxide reductase contributes to the maintenance of adhesins in three major pathogens","volume":"93","author":"Wizemann","year":"1996","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/S0969-2126(00)00526-8_BIB17","doi-asserted-by":"crossref","first-page":"5939","DOI":"10.1073\/pnas.90.13.5939","article-title":"Identification of an ethylene-responsive region in the promoter of a fruit ripening gene","volume":"90","author":"Montgomery","year":"1993","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/S0969-2126(00)00526-8_BIB18","doi-asserted-by":"crossref","first-page":"14167","DOI":"10.1074\/jbc.275.19.14167","article-title":"Identification and characterization of a putative active site for peptide methionine sulfoxide reductase (MsrA) and its substrate stereospecificity","volume":"275","author":"Moskovitz","year":"2000","journal-title":"J. Biol. Chem."},{"key":"10.1016\/S0969-2126(00)00526-8_BIB19","doi-asserted-by":"crossref","first-page":"6463","DOI":"10.1073\/pnas.97.12.6463","article-title":"Thiol-disulphide exchange is involved in the catalytic mechanism of peptide methionine sulfoxide reductase","volume":"97","author":"Lowther","year":"2000","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/S0969-2126(00)00526-8_BIB20","article-title":"A sulfenic acid enzyme intermediate is involved in the catalytic mechanism of Peptide Methionine Sulfoxide Reductase from Escherichia coli","volume":"in press","author":"Boschi-Muller","year":"2000","journal-title":"J. Biol. Chem."},{"key":"10.1016\/S0969-2126(00)00526-8_BIB21","doi-asserted-by":"crossref","first-page":"472","DOI":"10.1038\/355472a0","article-title":"The free R value","volume":"355","author":"Br\u00fcnger","year":"1992","journal-title":"Nature"},{"key":"10.1016\/S0969-2126(00)00526-8_BIB22","doi-asserted-by":"crossref","first-page":"282","DOI":"10.1107\/S0021889892009944","article-title":"Procheck","volume":"26","author":"Laskowski","year":"1993","journal-title":"J. Appl. Crystallogr."},{"key":"10.1016\/S0969-2126(00)00526-8_BIB23","doi-asserted-by":"crossref","first-page":"905","DOI":"10.1107\/S0907444998003254","article-title":"Crystallography & N.M.R. system","volume":"54","author":"Br\u00fcnger","year":"1998","journal-title":"Acta Crystallogr. D"},{"key":"10.1016\/S0969-2126(00)00526-8_BIB24","doi-asserted-by":"crossref","first-page":"909","DOI":"10.1016\/S0006-3495(65)86759-5","article-title":"Stereochemical criteria for polypeptide and protein chain conformation","volume":"5","author":"Ramakrishnan","year":"1965","journal-title":"Biophys. J."},{"key":"10.1016\/S0969-2126(00)00526-8_BIB25","doi-asserted-by":"crossref","first-page":"807","DOI":"10.1093\/protein\/12.10.807","article-title":"Skewed distribution of protein secondary structure contents over the conformational triangle","volume":"12","author":"Zhang","year":"1999","journal-title":"Protein Engineering"},{"key":"10.1016\/S0969-2126(00)00526-8_BIB26","doi-asserted-by":"crossref","first-page":"892","DOI":"10.1093\/bioinformatics\/14.10.892","article-title":"Jpred","volume":"14","author":"Cuff","year":"1998","journal-title":"Bioinformatics"},{"key":"10.1016\/S0969-2126(00)00526-8_BIB27","doi-asserted-by":"crossref","first-page":"235","DOI":"10.1093\/nar\/28.1.235","article-title":"The Protein Data Bank.","volume":"28","author":"Berman","year":"2000","journal-title":"Nucleic Acids Res."},{"key":"10.1016\/S0969-2126(00)00526-8_BIB28","doi-asserted-by":"crossref","first-page":"739","DOI":"10.1093\/protein\/11.9.739","article-title":"Protein structure alignment by incremental combinatorial extension (CE) of the optimal path","volume":"11","author":"Shindyalov","year":"1998","journal-title":"Protein Engineering"},{"key":"10.1016\/S0969-2126(00)00526-8_BIB29","doi-asserted-by":"crossref","first-page":"35","DOI":"10.1016\/S0969-2126(00)00078-2","article-title":"The crystal structure of the formiminotransferase-cyclodeaminase","volume":"8","author":"Kohls","year":"2000","journal-title":"Structure Fold Des."},{"key":"10.1016\/S0969-2126(00)00526-8_BIB30","doi-asserted-by":"crossref","first-page":"635","DOI":"10.1016\/S0969-2126(97)00219-0","article-title":"Formylmethanofuran","volume":"5","author":"Ermler","year":"1997","journal-title":"Structure Fold Des."},{"key":"10.1016\/S0969-2126(00)00526-8_BIB31","doi-asserted-by":"crossref","first-page":"3205","DOI":"10.1073\/pnas.93.8.3205","article-title":"Chromosomal localization of the mammalian peptide-methionine sulfoxide reductase gene and its differential expression in various tissues","volume":"93","author":"Moskovitz","year":"1996","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/S0969-2126(00)00526-8_BIB32","doi-asserted-by":"crossref","first-page":"235","DOI":"10.1046\/j.1365-313X.1996.10020235.x","article-title":"Identification of a peptide methionine sulphoxide reductase gene in an oleosin promoter from Brassica napus","volume":"10","author":"Sadanandom","year":"1996","journal-title":"Plant J."},{"key":"10.1016\/S0969-2126(00)00526-8_BIB33","doi-asserted-by":"crossref","first-page":"17","DOI":"10.1016\/S0014-5793(99)00917-5","article-title":"Molecular cloning and functional expression of a human peptide methionine sulfoxide reductase (hMsrA)","volume":"456","author":"Kuschel","year":"1999","journal-title":"FEBS Lett."},{"key":"10.1016\/S0969-2126(00)00526-8_BIB34","doi-asserted-by":"crossref","first-page":"4367","DOI":"10.1002\/j.1460-2075.1988.tb03335.x","article-title":"Pilin expression in Neisseria gonorrhoeae is under both positive and negative transcriptional control","volume":"7","author":"Taha","year":"1988","journal-title":"EMBO J."},{"key":"10.1016\/S0969-2126(00)00526-8_BIB35","doi-asserted-by":"crossref","first-page":"359","DOI":"10.1006\/jmbi.1998.2002","article-title":"Crystal structures of the catalytic domain of HIV-1 integrase free and complexed with its metal cofactor","volume":"282","author":"Maignan","year":"1998","journal-title":"J. Mol. Biol."},{"key":"10.1016\/S0969-2126(00)00526-8_BIB36","doi-asserted-by":"crossref","first-page":"1194","DOI":"10.1107\/S0907444900009483","article-title":"Crystallisation and preliminary X-ray diffraction studies of the peptide methionine sulfoxide reductase from Escherichia coli","volume":"56","author":"T\u00eate-Favier","year":"2000","journal-title":"Acta Crystallogr. D"},{"key":"10.1016\/S0969-2126(00)00526-8_BIB37","doi-asserted-by":"crossref","first-page":"149","DOI":"10.1016\/0079-6107(85)90001-X","article-title":"The role of the \u03b1 helix dipole in protein function and structure","volume":"45","author":"Hol","year":"1985","journal-title":"Prog. Biophys. Mol. Biol."},{"key":"10.1016\/S0969-2126(00)00526-8_BIB38","doi-asserted-by":"crossref","unstructured":"CCP4 (Collaborative Computational Project 4) (1994). The CCP4 suite: programs for protein crystallography. Acta Crystallogr. D 50, 760\u2013763.","DOI":"10.1107\/S0907444994003112"},{"key":"10.1016\/S0969-2126(00)00526-8_BIB39","first-page":"34","article-title":"Dm","volume":"31","author":"Cowtan","year":"1994","journal-title":"Joint CCP4 and ESF-EACBM Newsletter on Protein Crystallography"},{"key":"10.1016\/S0969-2126(00)00526-8_BIB40","doi-asserted-by":"crossref","first-page":"110","DOI":"10.1107\/S0108767390010224","article-title":"Improved methods for building protein models in electron density maps and for the location of errors in these models","volume":"47","author":"Jones","year":"1991","journal-title":"Acta Crystallogr. A"},{"key":"10.1016\/S0969-2126(00)00526-8_BIB41","series-title":"Silicon Graphics Geometry Partners Directory, vol. 81","article-title":"The TURBO-FRODO Graphics Package","author":"Roussel","year":"1992"},{"key":"10.1016\/S0969-2126(00)00526-8_BIB42","doi-asserted-by":"crossref","first-page":"45","DOI":"10.1093\/nar\/28.1.45","article-title":"The SWISS-PROT protein sequence database and its supplement TrEMBL in 2000","volume":"28","author":"Bairoch","year":"2000","journal-title":"Nucleic Acids Res."},{"key":"10.1016\/S0969-2126(00)00526-8_BIB43","doi-asserted-by":"crossref","first-page":"41","DOI":"10.1093\/nar\/28.1.41","article-title":"The Protein Information Resource (PIR)","volume":"28","author":"Barker","year":"2000","journal-title":"Nucleic Acids Res."},{"key":"10.1016\/S0969-2126(00)00526-8_BIB44","doi-asserted-by":"crossref","first-page":"12","DOI":"10.1093\/nar\/27.1.12","article-title":"GenBank","volume":"27","author":"Benson","year":"1999","journal-title":"Nucleic Acids Res."},{"key":"10.1016\/S0969-2126(00)00526-8_BIB45","doi-asserted-by":"crossref","first-page":"4673","DOI":"10.1093\/nar\/22.22.4673","article-title":"Clustalw","volume":"22","author":"Thompson","year":"1994","journal-title":"Nucleic Acids Res."},{"key":"10.1016\/S0969-2126(00)00526-8_BIB46","series-title":"Methods in Enzymology, vol. 276","doi-asserted-by":"crossref","DOI":"10.1016\/S0076-6879(97)76066-X","article-title":"Processing of X-ray diffraction data collected in oscillation mode","author":"Otwinowski","year":"1997"},{"key":"10.1016\/S0969-2126(00)00526-8_BIB47","doi-asserted-by":"crossref","first-page":"897","DOI":"10.1110\/ps.8.4.897","article-title":"Protein structural topology","volume":"8","author":"Westhead","year":"1999","journal-title":"Protein Sci."},{"key":"10.1016\/S0969-2126(00)00526-8_BIB48","first-page":"282","article-title":"Molscript","volume":"26","author":"Kraulis","year":"1991","journal-title":"J. Appl. Crystallogr."},{"key":"10.1016\/S0969-2126(00)00526-8_BIB49","doi-asserted-by":"crossref","first-page":"869","DOI":"10.1107\/S0907444994006396","article-title":"Raster3D version 2.4 \u2013 a program for photorealistic molecular graphics","volume":"50","author":"Meritt","year":"1994","journal-title":"Acta Crystallogr. D"},{"key":"10.1016\/S0969-2126(00)00526-8_BIB50","doi-asserted-by":"crossref","first-page":"305","DOI":"10.1093\/bioinformatics\/15.4.305","article-title":"ESPript","volume":"15","author":"Gouet","year":"1999","journal-title":"Bioinformatics"}],"container-title":["Structure"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0969212600005268?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0969212600005268?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2021,5,7]],"date-time":"2021-05-07T07:20:37Z","timestamp":1620372037000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0969212600005268"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2000,11]]},"references-count":50,"journal-issue":{"issue":"11","published-print":{"date-parts":[[2000,11]]}},"alternative-id":["S0969212600005268"],"URL":"https:\/\/doi.org\/10.1016\/s0969-2126(00)00526-8","relation":{},"ISSN":["0969-2126"],"issn-type":[{"value":"0969-2126","type":"print"}],"subject":[],"published":{"date-parts":[[2000,11]]}}}