{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2024,7,19]],"date-time":"2024-07-19T17:09:38Z","timestamp":1721408978156},"reference-count":44,"publisher":"Elsevier BV","issue":"1","license":[{"start":{"date-parts":[[2002,3,1]],"date-time":"2002-03-01T00:00:00Z","timestamp":1014940800000},"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":[[2002,3]]},"DOI":"10.1006\/jmbi.2002.5420","type":"journal-article","created":{"date-parts":[[2002,10,6]],"date-time":"2002-10-06T18:37:32Z","timestamp":1033929452000},"page":"109-117","source":"Crossref","is-referenced-by-count":16,"title":["Structure of an extended-spectrum class A \u03b2-lactamase from Proteus vulgaris K1"],"prefix":"10.1006","volume":"317","author":[{"given":"Michiyoshi","family":"Nukaga","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Kayoko","family":"Mayama","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Gregg V","family":"Crichlow","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"James R","family":"Knox","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"78","reference":[{"key":"10.1006\/jmbi.2002.5420_BIB1","doi-asserted-by":"crossref","first-page":"385","DOI":"10.1111\/j.1365-2958.1995.tb02404.x","article-title":"Beta-lactamases and bacterial resistance to antibiotics","volume":"16","author":"Frere","year":"1995","journal-title":"Mol. Microbiol."},{"key":"10.1006\/jmbi.2002.5420_BIB2","doi-asserted-by":"crossref","first-page":"162","DOI":"10.1021\/ar960007e","article-title":"Molecular bases for interactions between \u03b2-lactam antibiotics and \u03b2-lactamases","volume":"30","author":"Massova","year":"1997","journal-title":"Accts Chem. Res."},{"key":"10.1006\/jmbi.2002.5420_BIB3","doi-asserted-by":"crossref","first-page":"581","DOI":"10.1042\/bj3300581","article-title":"Catalytic properties of class A \u03b2-lactamases","volume":"330","author":"Matagne","year":"1998","journal-title":"Biochem. J."},{"key":"10.1006\/jmbi.2002.5420_BIB4","doi-asserted-by":"crossref","first-page":"269","DOI":"10.1042\/bj2760269","article-title":"A standard numbering scheme for class A \u03b2-lactamases","volume":"276","author":"Ambler","year":"1991","journal-title":"Biochem. J."},{"key":"10.1006\/jmbi.2002.5420_BIB5","doi-asserted-by":"crossref","first-page":"865","DOI":"10.2174\/1381612805666230112185101","article-title":"OXA-type \u03b2-lactamases","volume":"5","author":"Naas","year":"1999","journal-title":"Curr. Pharm. Des."},{"key":"10.1006\/jmbi.2002.5420_BIB6","doi-asserted-by":"crossref","first-page":"567","DOI":"10.1128\/jb.152.2.567-571.1982","article-title":"Characterization of eight \u03b2-lactamases of gram-negative bacteria","volume":"152","author":"Sawai","year":"1982","journal-title":"J. Bacteriol."},{"key":"10.1006\/jmbi.2002.5420_BIB7","doi-asserted-by":"crossref","first-page":"10200","DOI":"10.1021\/bi00199a049","article-title":"Replacement of serine 237 in class A \u03b2-lactamase of Proteus vulgaris modifies its unique substrate specificity","volume":"33","author":"Tamaki","year":"1994","journal-title":"Biochemistry"},{"key":"10.1006\/jmbi.2002.5420_BIB8","doi-asserted-by":"crossref","first-page":"1211","DOI":"10.1128\/AAC.39.6.1211","article-title":"A functional classification scheme for \u03b2-lactamases and its correlation with molecular structure","volume":"39","author":"Bush","year":"1995","journal-title":"Antimicrob. Agents Chemother."},{"key":"10.1006\/jmbi.2002.5420_BIB9","doi-asserted-by":"crossref","first-page":"31","DOI":"10.1016\/0167-4838(94)90048-5","article-title":"Chromosomally encoded cephalosporin-hydrolyzing \u03b2-lactamase of Proteus vulgaris RO104 belongs to Ambler\u2019s class A","volume":"1207","author":"Peduzzi","year":"1994","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1006\/jmbi.2002.5420_BIB10","doi-asserted-by":"crossref","first-page":"2269","DOI":"10.1128\/AAC.39.10.2269","article-title":"Cloning and sequence of the gene encoding a cefotaxime-hydrolyzing class A \u03b2-lactamase isolated from E. coli","volume":"39","author":"Ishii","year":"1995","journal-title":"Antimicrob. Agents Chemother."},{"key":"10.1006\/jmbi.2002.5420_BIB11","doi-asserted-by":"crossref","first-page":"2079","DOI":"10.1006\/jmbi.1998.2432","article-title":"Crystal structure of an extended-spectrum \u03b2-lactamase Toho-1 at 1.8 \u00c5 resolution","volume":"285","author":"Ibuka","year":"1999","journal-title":"J. Mol. Biol."},{"key":"10.1006\/jmbi.2002.5420_BIB12","doi-asserted-by":"crossref","first-page":"157","DOI":"10.1107\/S0108767393007597","article-title":"AMoRe","volume":"50","author":"Navaza","year":"1994","journal-title":"Acta Crystallog. sect. A"},{"key":"10.1006\/jmbi.2002.5420_BIB13","first-page":"905","article-title":"CNS (Crystallography and NMR System)","volume":"54","author":"Brunger","year":"1998","journal-title":"Acta Crystallog. sect. D"},{"key":"10.1006\/jmbi.2002.5420_BIB14","doi-asserted-by":"crossref","first-page":"224","DOI":"10.1016\/S0263-7855(98)80040-4","article-title":"CHAIN - a crystallographic modeling program","volume":"6","author":"Sack","year":"1988","journal-title":"J. Mol. Graph."},{"key":"10.1006\/jmbi.2002.5420_BIB15","doi-asserted-by":"crossref","first-page":"156","DOI":"10.1006\/jsbi.1999.4094","article-title":"XtalView\/Xfit - a versatile program for manipulating atomic coordinates and electron density","volume":"125","author":"McRee","year":"1999","journal-title":"J. Struct. Biol."},{"key":"10.1006\/jmbi.2002.5420_BIB16","doi-asserted-by":"crossref","first-page":"472","DOI":"10.1038\/355472a0","article-title":"Free R value","volume":"355","author":"Brunger","year":"1992","journal-title":"Nature"},{"key":"10.1006\/jmbi.2002.5420_BIB17","doi-asserted-by":"crossref","first-page":"713","DOI":"10.1006\/jmbi.2000.3597","article-title":"The ultrahigh resolution crystal structure of ribonuclease A containing an isoasparty residue","volume":"297","author":"Esposito","year":"2000","journal-title":"J. Mol. Biol."},{"key":"10.1006\/jmbi.2002.5420_BIB18","doi-asserted-by":"crossref","first-page":"165","DOI":"10.1006\/jmbi.1993.1571","article-title":"Structure of a phosphonate-inhibited \u03b2-lactamase","volume":"234","author":"Chen","year":"1993","journal-title":"J. Mol. Biol."},{"key":"10.1006\/jmbi.2002.5420_BIB19","doi-asserted-by":"crossref","first-page":"7435","DOI":"10.1021\/ja9609718","article-title":"Crystal structure of 6\u03b1-(hydroxymethyl)penicillanate complexed to the TEM-1 \u03b2-lactamase from Escherichia coli","volume":"118","author":"Maveyraud","year":"1996","journal-title":"J. Am. Chem. Soc."},{"key":"10.1006\/jmbi.2002.5420_BIB20","doi-asserted-by":"crossref","first-page":"1861","DOI":"10.1021\/bi0022745","article-title":"Inhibition of the SHV-1 \u03b2-lactamase by sulfones","volume":"40","author":"Kuzin","year":"2001","journal-title":"Biochemistry"},{"key":"10.1006\/jmbi.2002.5420_BIB21","doi-asserted-by":"crossref","first-page":"11257","DOI":"10.1073\/pnas.90.23.11257","article-title":"Evolution of an enzyme activity","volume":"90","author":"Lobkovsky","year":"1993","journal-title":"Proc. Natl Acad. Sci. USA"},{"key":"10.1006\/jmbi.2002.5420_BIB22","doi-asserted-by":"crossref","first-page":"700","DOI":"10.1038\/359700a0","article-title":"Molecular structure of the acyl-enzyme intermediate in \u03b2-lactam hydrolysis at 1.7 \u00c5 resolution","volume":"359","author":"Strynadka","year":"1992","journal-title":"Nature"},{"key":"10.1006\/jmbi.2002.5420_BIB23","doi-asserted-by":"crossref","first-page":"682","DOI":"10.1107\/S0907444994014496","article-title":"TEM1 \u03b2-lactamase structure solved by molecular replacement and refined structure of the S235A mutant","volume":"51","author":"Fonze","year":"1995","journal-title":"Acta Crystallog. sect. D"},{"key":"10.1006\/jmbi.2002.5420_BIB24","doi-asserted-by":"crossref","first-page":"5720","DOI":"10.1021\/bi990136d","article-title":"Structure of the SHV-1 \u03b2-lactamase","volume":"38","author":"Kuzin","year":"1999","journal-title":"Biochemistry"},{"key":"10.1006\/jmbi.2002.5420_BIB25","doi-asserted-by":"crossref","first-page":"3690","DOI":"10.1016\/S0021-9258(18)53748-0","article-title":"The role of Ser238 and Lys240 in the hydrolysis of third-generation cephalosporins by SHV-type \u03b2-lactamases probed by site-directed mutagenesis and three-dimensional modeling","volume":"268","author":"Huletsky","year":"1993","journal-title":"J. Biol. Chem."},{"key":"10.1006\/jmbi.2002.5420_BIB26","doi-asserted-by":"crossref","first-page":"625","DOI":"10.1006\/jmbi.1994.1756","article-title":"TEM \u03b2-lactamase mutants hydrolysing third-generation cephalosporins","volume":"244","author":"Raquet","year":"1994","journal-title":"J. Mol. Biol."},{"key":"10.1006\/jmbi.2002.5420_BIB27","doi-asserted-by":"crossref","first-page":"2593","DOI":"10.1128\/AAC.39.12.2593","article-title":"Extended-spectrum and inhibitor-resistant TEM-type \u03b2 -lactamases","volume":"39","author":"Knox","year":"1995","journal-title":"Antimicrob. Agents Chemother."},{"key":"10.1006\/jmbi.2002.5420_BIB28","doi-asserted-by":"crossref","first-page":"3286","DOI":"10.1021\/bi972127f","article-title":"Role of the omega-loop in the activity, substrate specificity, and structure of class A \u03b2-lactamase","volume":"37","author":"Banerjee","year":"1998","journal-title":"Biochemistry"},{"key":"10.1006\/jmbi.2002.5420_BIB29","doi-asserted-by":"crossref","first-page":"28075","DOI":"10.1074\/jbc.M003802200","article-title":"The high resolution crystal structure for class A \u03b2-lactamase PER-1 reveals the bases for its increase in breadth of activity","volume":"36","author":"Tranier","year":"2000","journal-title":"J. Biol. Chem."},{"key":"10.1006\/jmbi.2002.5420_BIB30","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1039\/a705983c","article-title":"The \u03b2-lactamase cycle","volume":"16","author":"Matagne","year":"1999","journal-title":"Nature Prod. Rep."},{"key":"10.1006\/jmbi.2002.5420_BIB31","doi-asserted-by":"crossref","first-page":"701","DOI":"10.1016\/0022-2836(91)90527-D","article-title":"Refined crystal structure of \u03b2-lactamase from Staphylococcus aureus PC1 at 2.0 \u00c5 resolution","volume":"217","author":"Herzberg","year":"1991","journal-title":"J. Mol. Biol."},{"key":"10.1006\/jmbi.2002.5420_BIB32","doi-asserted-by":"crossref","first-page":"399","DOI":"10.1042\/bj2710399","article-title":"Role of the conserved amino acids of the \u201cSDN\u201d loop in a class A \u03b2-lactamase studied by site-directed mutagenesis","volume":"271","author":"Jacob","year":"1990","journal-title":"Biochem. J."},{"key":"10.1006\/jmbi.2002.5420_BIB33","doi-asserted-by":"crossref","first-page":"213","DOI":"10.1042\/bj2790213","article-title":"Mechanism of acyl transfer by the class A serine \u03b2-lactamase of Streptomyces albus G","volume":"279","author":"Lamotte-Brasseur","year":"1991","journal-title":"Biochem. J."},{"key":"10.1006\/jmbi.2002.5420_BIB34","doi-asserted-by":"crossref","first-page":"693","DOI":"10.1093\/protein\/5.7.693","article-title":"Site-saturation mutagenesis and three-dimensional modelling of ROB-1 define a substrate binding role of Ser130 in class A \u03b2-lactamases","volume":"5","author":"Juteau","year":"1992","journal-title":"Protein Eng."},{"key":"10.1006\/jmbi.2002.5420_BIB35","doi-asserted-by":"crossref","first-page":"275","DOI":"10.1002\/prot.340060310","article-title":"Substrate specificities in class A \u03b2-lactamases. Preference for penams vs cephems. The role of residue 237","volume":"6","author":"Healey","year":"1989","journal-title":"Proteins: Struct. Funct. Genet."},{"key":"10.1006\/jmbi.2002.5420_BIB36","doi-asserted-by":"crossref","first-page":"937","DOI":"10.1016\/S1074-5521(96)90182-9","article-title":"Molecular evolution of bacterial \u03b2-lactam resistance","volume":"3","author":"Knox","year":"1996","journal-title":"Chem. Biol."},{"key":"10.1006\/jmbi.2002.5420_BIB37","doi-asserted-by":"crossref","first-page":"9532","DOI":"10.1021\/bi00029a030","article-title":"Binding of cephalothin and cefotaxime to D-ala-D-ala peptidase reveals a functional basis of a natural mutation in a low-affinity penicillin-binding protein and in extended-spectrum \u03b2-lactamases","volume":"34","author":"Kuzin","year":"1995","journal-title":"Biochemistry"},{"key":"10.1006\/jmbi.2002.5420_BIB38","doi-asserted-by":"crossref","first-page":"4435","DOI":"10.1021\/ja00064a003","article-title":"Inactivation of class A \u03b2-lactamases by clavulanic acid","volume":"115","author":"Imtiaz","year":"1993","journal-title":"J. Am. Chem. Soc."},{"key":"10.1006\/jmbi.2002.5420_BIB39","doi-asserted-by":"crossref","first-page":"435","DOI":"10.1016\/0022-2836(91)90023-Y","article-title":"Beta-lactamase of Bacillus licheniformis","volume":"220","author":"Knox","year":"1991","journal-title":"J. Mol. Biol."},{"key":"10.1006\/jmbi.2002.5420_BIB40","doi-asserted-by":"crossref","first-page":"364","DOI":"10.1002\/prot.340160406","article-title":"Crystal structure of E. coli TEM1 \u03b2-lactamase at 1.8 \u00c5 resolution","volume":"16","author":"Jelsch","year":"1993","journal-title":"Proteins: Struct. Funct. Genet."},{"key":"10.1006\/jmbi.2002.5420_BIB41","doi-asserted-by":"crossref","first-page":"2207","DOI":"10.1021\/jm9506027","article-title":"Modeling study on a hydrolytic mechanism of class A \u03b2-lactamases","volume":"39","author":"Ishiguro","year":"1996","journal-title":"J. Med. Chem."},{"key":"10.1006\/jmbi.2002.5420_BIB42","doi-asserted-by":"crossref","first-page":"15","DOI":"10.1111\/j.1432-1033.1990.tb15365.x","article-title":"Role of lysine-67 in the active site of class C \u03b2-lactamase from Citrobacter freundii GN346","volume":"188","author":"Tsukamoto","year":"1990","journal-title":"Eur. J. Biochem."},{"key":"10.1006\/jmbi.2002.5420_BIB43","doi-asserted-by":"crossref","first-page":"505","DOI":"10.1016\/S0076-6879(97)77028-9","article-title":"Raster3D","volume":"277","author":"Merritt","year":"1997","journal-title":"Methods Enzymol."},{"key":"10.1006\/jmbi.2002.5420_BIB44","doi-asserted-by":"crossref","first-page":"946","DOI":"10.1107\/S0021889891004399","article-title":"MOLSCRIPT","volume":"24","author":"Kraulis","year":"1991","journal-title":"J. Appl. Crystallog."}],"container-title":["Journal of Molecular Biology"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0022283602954203?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0022283602954203?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2023,4,4]],"date-time":"2023-04-04T06:48:53Z","timestamp":1680590933000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0022283602954203"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2002,3]]},"references-count":44,"journal-issue":{"issue":"1","published-print":{"date-parts":[[2002,3]]}},"alternative-id":["S0022283602954203"],"URL":"https:\/\/doi.org\/10.1006\/jmbi.2002.5420","relation":{},"ISSN":["0022-2836"],"issn-type":[{"value":"0022-2836","type":"print"}],"subject":[],"published":{"date-parts":[[2002,3]]}}}