{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,8,21]],"date-time":"2026-08-21T13:18:03Z","timestamp":1787318283957,"version":"build-2736575974"},"reference-count":40,"publisher":"Wiley","issue":"6","license":[{"start":{"date-parts":[[2015,2,6]],"date-time":"2015-02-06T00:00:00Z","timestamp":1423180800000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"funder":[{"name":"Norwegian Structural Biology Centre"},{"DOI":"10.13039\/501100005416","name":"Research Council of Norway","doi-asserted-by":"crossref","id":[{"id":"10.13039\/501100005416","id-type":"DOI","asserted-by":"crossref"}]},{"name":"FRIMEDBIO","award":["213808"],"award-info":[{"award-number":["213808"]}]},{"name":"Troms\u00f8 Research Foundation"}],"content-domain":{"domain":["febs.onlinelibrary.wiley.com"],"crossmark-restriction":true},"short-container-title":["The FEBS Journal"],"published-print":{"date-parts":[[2015,3]]},"abstract":"<jats:p>\n                    During the last decades antimicrobial resistance has become a global health problem. Metallo\u2010\u03b2\u2010lactamases (\n                    <jats:styled-content style=\"fixed-case\">MBL<\/jats:styled-content>\n                    s) which are broad\u2010spectrum \u03b2\u2010lactamases that inactivate virtually all \u03b2\u2010lactams including carbapenems, are contributing to this health problem. In this study a novel\n                    <jats:styled-content style=\"fixed-case\">MBL<\/jats:styled-content>\n                    variant, termed\n                    <jats:styled-content style=\"fixed-case\">VIM<\/jats:styled-content>\n                    \u201026, identified in a\n                    <jats:italic>Klebsiella\u00a0pneumoniae<\/jats:italic>\n                    isolate was studied.\n                    <jats:styled-content style=\"fixed-case\">VIM<\/jats:styled-content>\n                    \u201026 belongs to the Verona integron\u2010encoded metallo\u2010\u03b2\u2010lactamase (\n                    <jats:styled-content style=\"fixed-case\">VIM<\/jats:styled-content>\n                    ) family of\n                    <jats:styled-content style=\"fixed-case\">MBL<\/jats:styled-content>\n                    s and is a His224Leu variant of the well\u2010characterized\n                    <jats:styled-content style=\"fixed-case\">VIM<\/jats:styled-content>\n                    \u20101 variant. In this study, we report the kinetic parameters, minimum inhibitory concentrations and crystal structures of a recombinant\n                    <jats:styled-content style=\"fixed-case\">VIM<\/jats:styled-content>\n                    \u201026 protein, and compare them to previously published data on\n                    <jats:styled-content style=\"fixed-case\">VIM<\/jats:styled-content>\n                    \u20101,\n                    <jats:styled-content style=\"fixed-case\">VIM<\/jats:styled-content>\n                    \u20102 and\n                    <jats:styled-content style=\"fixed-case\">VIM<\/jats:styled-content>\n                    \u20107. The kinetic parameters and minimum inhibitory concentration determinations show that\n                    <jats:styled-content style=\"fixed-case\">VIM<\/jats:styled-content>\n                    \u201026, like\n                    <jats:styled-content style=\"fixed-case\">VIM<\/jats:styled-content>\n                    \u20107, has higher penicillinase activity but lower cephalosporinase activity than\n                    <jats:styled-content style=\"fixed-case\">VIM<\/jats:styled-content>\n                    \u20101 and\n                    <jats:styled-content style=\"fixed-case\">VIM<\/jats:styled-content>\n                    \u20102. The four determined\n                    <jats:styled-content style=\"fixed-case\">VIM<\/jats:styled-content>\n                    \u201026 crystal structures revealed mono\u2010 and di\u2010zinc forms, where the Zn1 ion has distorted tetrahedral coordination geometry with an additional water molecule (W2) at a distance of 2.6\u20133.7 \u00c5, which could be important during catalysis. The R2 drug binding site in\n                    <jats:styled-content style=\"fixed-case\">VIM<\/jats:styled-content>\n                    \u201026 is more open compared to\n                    <jats:styled-content style=\"fixed-case\">VIM<\/jats:styled-content>\n                    \u20102 and\n                    <jats:styled-content style=\"fixed-case\">VIM<\/jats:styled-content>\n                    \u20107 and neutrally charged due to Leu224 and Ser228. Thus, the\n                    <jats:styled-content style=\"fixed-case\">VIM<\/jats:styled-content>\n                    \u201026 drug binding properties are different from the\n                    <jats:styled-content style=\"fixed-case\">VIM<\/jats:styled-content>\n                    \u20102 (Tyr224\/Arg228) and\n                    <jats:styled-content style=\"fixed-case\">VIM<\/jats:styled-content>\n                    \u20107 (His224\/Arg228) structures, indicating a role of these residues in the substrate specificity.\n                  <\/jats:p>","DOI":"10.1111\/febs.13200","type":"journal-article","created":{"date-parts":[[2015,1,19]],"date-time":"2015-01-19T10:12:07Z","timestamp":1421662327000},"page":"1031-1042","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":24,"title":["Structural and biochemical characterization of\n                    <scp>VIM<\/scp>\n                    \u201026 shows that Leu224 has implications for the substrate specificity of\n                    <scp>VIM<\/scp>\n                    metallo\u2010\u03b2\u2010lactamases"],"prefix":"10.1111","volume":"282","author":[{"given":"Hanna\u2010Kirsti S.","family":"Leiros","sequence":"first","affiliation":[{"name":"Norwegian Structural Biology Centre Department of Chemistry UiT The Arctic University of Norway Troms\u00f8 Norway"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Kine Susann Waade","family":"Edvardsen","sequence":"additional","affiliation":[{"name":"Norwegian Structural Biology Centre Department of Chemistry UiT The Arctic University of Norway Troms\u00f8 Norway"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Gro Elin Kj\u00e6reng","family":"Bjerga","sequence":"additional","affiliation":[{"name":"Norwegian Structural Biology Centre Department of Chemistry UiT The Arctic University of Norway Troms\u00f8 Norway"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"\u00d8rjan","family":"Samuelsen","sequence":"additional","affiliation":[{"name":"Norwegian National Advisory Unit on Detection of Antimicrobial Resistance Department of Microbiology and Infection Control University Hospital of North Norway Troms\u00f8 Norway"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"311","published-online":{"date-parts":[[2015,2,6]]},"reference":[{"key":"e_1_2_8_2_1","unstructured":"WHO(2014)World Health Organization: Antimicrobial resistance: globalreport on surveillance 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