{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,11,9]],"date-time":"2025-11-09T07:42:28Z","timestamp":1762674148575},"reference-count":25,"publisher":"Wiley","issue":"23","license":[{"start":{"date-parts":[[2016,11,6]],"date-time":"2016-11-06T00:00:00Z","timestamp":1478390400000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/501100000265","name":"Medical Research Council","doi-asserted-by":"publisher","award":["MR\/M026647\/1"],"award-info":[{"award-number":["MR\/M026647\/1"]}],"id":[{"id":"10.13039\/501100000265","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["febs.onlinelibrary.wiley.com"],"crossmark-restriction":true},"short-container-title":["The FEBS Journal"],"published-print":{"date-parts":[[2016,12]]},"abstract":"<jats:sec><jats:label \/><jats:p>Several soil\u2010derived Actinobacteria produce secondary metabolites that are proven specific and potent inhibitors of the human angiotensin\u2010I\u2010converting enzyme (ACE), a key target for the modulation of hypertension through its role in the renin\u2013angiotensin\u2013aldosterone system. K\u201026\u2010DCP is a zinc dipeptidyl carboxypeptidase (DCP) produced by <jats:italic>Astrosporangium hypotensionis<\/jats:italic>, and an ancestral homologue of ACE. Here we report the high\u2010resolution crystal structures of K\u201026\u2010DCP and of its complex with the natural microbial tripeptide product K\u201026. The experimental results provide the structural basis for better understanding the specificity of K\u201026 for human ACE over bacterial DCPs.<\/jats:p><\/jats:sec><jats:sec><jats:title>Database<\/jats:title><jats:p>Structural data are available in the PDB under the accession numbers <jats:ext-link xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" xlink:href=\"http:\/\/www.rcsb.org\/pdb\/search\/structidSearch.do?structureId=5L43\">5L43<\/jats:ext-link> and <jats:ext-link xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" xlink:href=\"http:\/\/www.rcsb.org\/pdb\/search\/structidSearch.do?structureId=5L44\">5L44<\/jats:ext-link>.<\/jats:p><\/jats:sec>","DOI":"10.1111\/febs.13928","type":"journal-article","created":{"date-parts":[[2016,10,18]],"date-time":"2016-10-18T15:31:23Z","timestamp":1476804683000},"page":"4357-4369","update-policy":"http:\/\/dx.doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":8,"title":["Crystal structure of a peptidyl\u2010dipeptidase K\u201026\u2010DCP from <i>Actinomycete<\/i> in complex with its natural inhibitor"],"prefix":"10.1111","volume":"283","author":[{"given":"Geoffrey","family":"Masuyer","sequence":"first","affiliation":[{"name":"Department of Biology and Biochemistry University of Bath UK"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Gyles E.","family":"Cozier","sequence":"additional","affiliation":[{"name":"Department of Biology and Biochemistry University of Bath UK"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Glenna J.","family":"Kramer","sequence":"additional","affiliation":[{"name":"Department of Chemistry Vanderbilt University Nashville TN USA"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Brian O.","family":"Bachmann","sequence":"additional","affiliation":[{"name":"Department of Chemistry Vanderbilt University Nashville TN USA"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"K. 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