{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,10,12]],"date-time":"2025-10-12T20:02:25Z","timestamp":1760299345374,"version":"3.33.0"},"reference-count":35,"publisher":"International Union of Crystallography (IUCr)","issue":"5","license":[{"start":{"date-parts":[[2016,4,26]],"date-time":"2016-04-26T00:00:00Z","timestamp":1461628800000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/journals.iucr.org\/services\/copyrightpolicy.html"},{"start":{"date-parts":[[2016,4,26]],"date-time":"2016-04-26T00:00:00Z","timestamp":1461628800000},"content-version":"tdm","delay-in-days":0,"URL":"http:\/\/journals.iucr.org\/services\/copyrightpolicy.html#TDM"}],"content-domain":{"domain":["iucr.org","wiley.com","iucrj.org"],"crossmark-restriction":true},"short-container-title":["Acta Crystallogr D Struct Biol","Acta Crystallogr D","Acta Cryst D","Acta Cryst D Struct Biol","Acta Cryst Sect D","Acta Cryst Sect D Struct Biol","Acta Crystallogr Sect D","Acta Crystallogr Sect D Struct Biol","Acta Crystallogr D Biol Crystallogr","Acta Cryst D Biol Cryst"],"published-print":{"date-parts":[[2016,5,1]]},"abstract":"<jats:p>The prolyl 4-hydroxylases (P4Hs) are mononuclear nonheme iron enzymes that catalyze the formation of 4<jats:italic>R<\/jats:italic>-hydroxyproline from many different substrates, with various biological implications. P4H is a key player in collagen accumulation, which has implications in fibrotic disorders. The stabilization of collagen triple-helical structure<jats:italic>via<\/jats:italic>prolyl hydroxylation is the rate-limiting step in collagen biosynthesis, and therefore P4H has been extensively investigated as a potential therapeutic target of fibrotic disease. Understanding how these enzymes recognize cofactors and substrates is important and will aid in the future design of inhibitors of P4H. In this article, X-ray crystal structures of a metallocofactor- and \u03b1-ketoglutarate (\u03b1KG)-bound form of P4H from<jats:italic>Bacillus anthracis<\/jats:italic>(BaP4H) are reported. Structures of BaP4H were solved at 1.63 and 2.35\u2005\u00c5 resolution and contained a cadmium ion and \u03b1KG bound in the active site. The \u03b1KG\u2013Cd\u2013BaP4H ternary complex reveals conformational changes of conserved residues upon the binding of metal ion and \u03b1KG, resulting in a closed active-site configuration required for dioxygen, substrate binding and catalysis.<\/jats:p>","DOI":"10.1107\/s2059798316004198","type":"journal-article","created":{"date-parts":[[2016,4,26]],"date-time":"2016-04-26T13:26:40Z","timestamp":1461677200000},"page":"675-681","update-policy":"https:\/\/doi.org\/10.1107\/cm_01","source":"Crossref","is-referenced-by-count":8,"title":["Structural analysis of cofactor binding for a prolyl 4-hydroxylase from the pathogenic bacterium<i>Bacillus anthracis<\/i>"],"prefix":"10.1107","volume":"72","author":[{"given":"Nicholas J.","family":"Schnicker","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Mishtu","family":"Dey","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"329","published-online":{"date-parts":[[2016,4,26]]},"reference":[{"key":"mn5109_bb1","doi-asserted-by":"crossref","first-page":"3542","DOI":"10.1021\/ja00009a048","volume":"113","author":"Adefarati","year":"1991","journal-title":"J. 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