{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,4]],"date-time":"2026-10-04T02:25:18Z","timestamp":1791080718987,"version":"4.1.0"},"reference-count":63,"publisher":"American Society for Microbiology","issue":"8","license":[{"start":{"date-parts":[[2012,8,1]],"date-time":"2012-08-01T00:00:00Z","timestamp":1343779200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/journals.asm.org\/non-commercial-tdm-license"}],"content-domain":{"domain":["journals.asm.org"],"crossmark-restriction":true},"short-container-title":["Antimicrob Agents Chemother"],"published-print":{"date-parts":[[2012,8]]},"abstract":"<jats:title>ABSTRACT<\/jats:title>\n                  <jats:p>\n                    Metallo-\u03b2-lactamase (MBL) genes confer resistance to virtually all \u03b2-lactam antibiotics and are rapidly disseminated by mobile genetic elements in Gram-negative bacteria. MBLs belong to three different subgroups, B1, B2, and B3, with the mobile MBLs largely confined to subgroup B1. The B3 MBLs are a divergent subgroup of predominantly chromosomally encoded enzymes. AIM-1 (\n                    <jats:underline>A<\/jats:underline>\n                    delaide\n                    <jats:underline>IM<\/jats:underline>\n                    ipenmase 1) from\n                    <jats:named-content xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" content-type=\"genus-species\" xlink:type=\"simple\">Pseudomonas aeruginosa<\/jats:named-content>\n                    was the first B3 MBL to be identified on a readily mobile genetic element. Here we present the crystal structure of AIM-1 and use\n                    <jats:italic>in silico<\/jats:italic>\n                    docking and quantum mechanics and molecular mechanics (QM\/MM) calculations, together with site-directed mutagenesis, to investigate its interaction with \u03b2-lactams. AIM-1 adopts the characteristic \u03b1\u03b2\/\u03b2\u03b1 sandwich fold of MBLs but differs from other B3 enzymes in the conformation of an active site loop (residues 156 to 162) which is involved both in disulfide bond formation and, we suggest, interaction with substrates. The structure, together with docking and QM\/MM calculations, indicates that the AIM-1 substrate binding site is narrower and more restricted than those of other B3 MBLs, possibly explaining its higher catalytic efficiency. The location of Gln157 adjacent to the AIM-1 zinc center suggests a role in drug binding that is supported by our\n                    <jats:italic>in silico<\/jats:italic>\n                    studies. However, replacement of this residue by either Asn or Ala resulted in only modest reductions in AIM-1 activity against the majority of \u03b2-lactam substrates, indicating that this function is nonessential. Our study reveals AIM-1 to be a subclass B3 MBL with novel structural and mechanistic features.\n                  <\/jats:p>","DOI":"10.1128\/aac.00448-12","type":"journal-article","created":{"date-parts":[[2012,6,5]],"date-time":"2012-06-05T05:54:33Z","timestamp":1338875673000},"page":"4341-4353","update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":61,"title":["Crystal Structure of the Mobile Metallo-\u03b2-Lactamase AIM-1 from Pseudomonas aeruginosa: Insights into Antibiotic Binding and the Role of Gln157"],"prefix":"10.1128","volume":"56","author":[{"given":"Hanna-Kirsti S.","family":"Leiros","sequence":"first","affiliation":[{"name":"The Norwegian Structural Biology Centre (NorStruct), Department of Chemistry, University of Troms\u00f8, Troms\u00f8, Norway"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Pardha S.","family":"Borra","sequence":"additional","affiliation":[{"name":"Research Group for Host-Microbe Interactions, Department of Medical Biology, Faculty of Health Sciences, University of Troms\u00f8, Troms\u00f8, Norway"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Bj\u00f8rn Olav","family":"Brandsdal","sequence":"additional","affiliation":[{"name":"The Norwegian Structural Biology Centre (NorStruct), Department of Chemistry, University of Troms\u00f8, Troms\u00f8, Norway"},{"name":"The Centre for Theoretical and Computational Chemistry, Department of Chemistry, University of Troms\u00f8, Troms\u00f8, Norway"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Kine Susann Waade","family":"Edvardsen","sequence":"additional","affiliation":[{"name":"The Norwegian Structural Biology Centre (NorStruct), Department of Chemistry, University of Troms\u00f8, Troms\u00f8, Norway"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"James","family":"Spencer","sequence":"additional","affiliation":[{"name":"School of Cellular and Molecular Medicine, University of Bristol, Bristol, United Kingdom"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Timothy R.","family":"Walsh","sequence":"additional","affiliation":[{"name":"Section of Medical Microbiology IIB, School of Medical Sciences, Cardiff University, Heath Park Hospital, Cardiff, United Kingdom"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"\u00d8rjan","family":"Samuelsen","sequence":"additional","affiliation":[{"name":"Reference Centre for Detection of Antimicrobial Resistance, Department of Microbiology and Infection Control, University Hospital of North Norway, Troms\u00f8, Norway"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"235","reference":[{"key":"e_1_3_3_2_2","doi-asserted-by":"crossref","first-page":"43","DOI":"10.1007\/s00214-002-0413-3","article-title":"Evaluation of an ab initio quantum mechanical\/molecular mechanical hybrid-potential link-atom method","volume":"109","author":"Amara P","year":"2003","unstructured":"AmaraP FieldMJ. 2003. 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