{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,11,1]],"date-time":"2026-11-01T07:07:55Z","timestamp":1793516875727,"version":"4.5.0"},"reference-count":47,"publisher":"Wiley","issue":"8","license":[{"start":{"date-parts":[[2011,4,20]],"date-time":"2011-04-20T00:00:00Z","timestamp":1303257600000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":["faseb.onlinelibrary.wiley.com"],"crossmark-restriction":true},"short-container-title":["The FASEB Journal"],"published-print":{"date-parts":[[2011,8]]},"abstract":"<jats:title>ABSTRACT<\/jats:title>\n                  <jats:sec>\n                    <jats:label\/>\n                    <jats:p>\n                      Metallo\u2010\u03b2\u2010lactamases (MBLs) hydrolyze most \u03b2\u2010lactam antibiotics, and bacteria containing this kind of enzyme pose a serious threat to the public health. The newly identified New Delhi MBL (NDM\u20101) is a new member of this family that shows tight binding to penicillin and cephalosporins. The rapid dissemination of\n                      <jats:italic>NDM\u20101<\/jats:italic>\n                      in clinically relevant bacteria has become a global concern. However, no clinically useful inhibitors against MBLs exist, partly due to the lack of knowledge about the catalysis mechanism of this kind of enzyme. Here we report the crystal structure of this novel enzyme in complex with a hydrolyzed ampicillin at its active site at 1.3\u2010\u00c5 resolution. Structural comparison with other MBLs revealed a new hydrolysis mechanism applicable to all three subclasses of MBLs, which might help the design of mechanism based inhibitors.\u2014Zhang, H.\u2010M., Hao, Q. Crystal structure of NDM\u20101 reveals a common \u03b2\u2010lactam hydrolysis mechanism.\n                      <jats:italic>FASEB J.<\/jats:italic>\n                      25, 2574\u20132582 (2011).\n                      <jats:ext-link xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" xlink:href=\"http:\/\/www.fasebj.org\">www.fasebj.org<\/jats:ext-link>\n                    <\/jats:p>\n                  <\/jats:sec>","DOI":"10.1096\/fj.11-184036","type":"journal-article","created":{"date-parts":[[2011,4,21]],"date-time":"2011-04-21T20:14:22Z","timestamp":1303416862000},"page":"2574-2582","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":238,"title":["Crystal structure of NDM\u20101 reveals a common \u03b2\u2010lactam hydrolysis mechanism"],"prefix":"10.1096","volume":"25","author":[{"given":"gMin","family":"Zhang","sequence":"first","affiliation":[{"name":"Department of Physiology University of Hong Kong Hong Kong China"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Quan","family":"Hao","sequence":"additional","affiliation":[{"name":"Department of Physiology University of Hong Kong Hong Kong China"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"311","published-online":{"date-parts":[[2011,4,20]]},"reference":[{"key":"e_1_2_5_2_1","doi-asserted-by":"publisher","DOI":"10.1128\/CMR.00037-09"},{"key":"e_1_2_5_3_1","doi-asserted-by":"publisher","DOI":"10.1021\/cr030102i"},{"key":"e_1_2_5_4_1","doi-asserted-by":"crossref","first-page":"895","DOI":"10.2174\/1381612805666230112192319","article-title":"The reactivity of beta\u2010lactams, the mechanism of catalysis and the inhibition of beta\u2010lactamases","volume":"5","author":"Page M. 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