{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,4,4]],"date-time":"2026-04-04T14:00:13Z","timestamp":1775311213038,"version":"3.50.1"},"reference-count":79,"publisher":"Wiley","issue":"5","license":[{"start":{"date-parts":[[2024,12,26]],"date-time":"2024-12-26T00:00:00Z","timestamp":1735171200000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":["onlinelibrary.wiley.com"],"crossmark-restriction":true},"short-container-title":["Proteins"],"published-print":{"date-parts":[[2025,5]]},"abstract":"<jats:title>ABSTRACT<\/jats:title>\n                  <jats:p>\n                    <jats:styled-content style=\"fixed-case\">\n                      <jats:italic>Staphylococcus aureus<\/jats:italic>\n                    <\/jats:styled-content>\n                    is a major cause of infections like bacteremia, pneumonia, and endocarditis. These infections are often linked to the ability of\n                    <jats:styled-content style=\"fixed-case\">\n                      <jats:italic>S. aureus<\/jats:italic>\n                    <\/jats:styled-content>\n                    to form biofilms. Several\n                    <jats:styled-content style=\"fixed-case\">\n                      <jats:italic>S. aureus<\/jats:italic>\n                    <\/jats:styled-content>\n                    serine hydrolases have previously been identified to be active during biofilm\u2010forming conditions. Here, we present the biochemical characterization of two of these enzymes\u2014fluorophosphonate binding hydrolase H and I (FphH, FphI). Cryogenic and room\u2010temperature X\u2010ray crystallography, enzymatic substrate profiling, small\u2010angle X\u2010ray scattering analysis, and molecular dynamics simulations provide new insights into similarities and differences between these two hydrolase_4 domain family members. We discover that these enzymes share an overall fold, including a flexible lid or cap region above the active site, which can be seen to be mobile in solution. Differences in the active site pocket and lid residues differentiate them and explain speed differences in their carboxyesterase substrate profile toward small unbranched carbon chain ester molecules. The first analysis of FphI is also compared to our previous knowledge of FphH and its association to stress conditions. These results enable the future precise targeting of Fph serine hydrolase family members with a long\u2010term goal to significantly improve the health and wellbeing of individuals and populations worldwide.\n                  <\/jats:p>","DOI":"10.1002\/prot.26785","type":"journal-article","created":{"date-parts":[[2024,12,27]],"date-time":"2024-12-27T01:21:07Z","timestamp":1735262467000},"page":"1009-1021","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":5,"title":["Similar but Distinct\u2014Biochemical Characterization of the\u00a0\n                    <scp>\n                      <i>Staphylococcus aureus<\/i>\n                    <\/scp>\n                    Serine Hydrolases\n                    <scp>FphH<\/scp>\n                    \u00a0and\n                    <scp>FphI<\/scp>"],"prefix":"10.1002","volume":"93","author":[{"ORCID":"https:\/\/orcid.org\/0000-0003-3192-6984","authenticated-orcid":false,"given":"Matthias","family":"Fellner","sequence":"first","affiliation":[{"name":"Biochemistry Department School of Biomedical Sciences, University of Otago  Dunedin New Zealand"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"George","family":"Randall","sequence":"additional","affiliation":[{"name":"Biochemistry Department School of Biomedical Sciences, University of Otago  Dunedin New Zealand"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Ianah R. 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G.","family":"Bitac","sequence":"additional","affiliation":[{"name":"Biochemistry Department School of Biomedical Sciences, University of Otago  Dunedin New Zealand"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Annmaree K.","family":"Warrender","sequence":"additional","affiliation":[{"name":"Australian Nuclear Science and Technology Organisation (ANSTO), Australian Synchrotron  Clayton Victoria Australia"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Ashish","family":"Sethi","sequence":"additional","affiliation":[{"name":"Australian Nuclear Science and Technology Organisation (ANSTO), Australian Synchrotron  Clayton Victoria Australia"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Raz","family":"Jelinek","sequence":"additional","affiliation":[{"name":"Ilse Katz Institute for Nanoscale Science and Technology (IKI), Ben\u2010Gurion University of the Negev  Beer\u2010Sheva Israel"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Itamar","family":"Kass","sequence":"additional","affiliation":[{"name":"Ilse Katz Institute for Nanoscale Science and Technology (IKI), Ben\u2010Gurion University of the Negev  Beer\u2010Sheva 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