{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,4,11]],"date-time":"2026-04-11T18:12:30Z","timestamp":1775931150863,"version":"3.50.1"},"reference-count":67,"publisher":"Wiley","issue":"11","license":[{"start":{"date-parts":[[2009,1,16]],"date-time":"2009-01-16T00:00:00Z","timestamp":1232064000000},"content-version":"vor","delay-in-days":5920,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Protein Science"],"published-print":{"date-parts":[[1992,11]]},"abstract":"<jats:title>Abstract<\/jats:title><jats:p>The structures of the oxidized and reduced forms of the rubredoxin from the archaebacterium, <jats:italic>Pyrococcus furiosus<\/jats:italic>, an organism that grows optimally at 100 \u00b0C, have been determined by X\u2010ray crystallography to a resolution of 1.8 \u00e5. Crystals of this rubredoxin grow in space group P2<jats:sub>1<\/jats:sub>2<jats:sub>1<\/jats:sub>2<jats:sub>1<\/jats:sub> with room temperature cell dimensions <jats:italic>a<\/jats:italic> = 34.6 \u00e5, <jats:italic>b<\/jats:italic> = 35.5 \u00e5, and <jats:italic>c<\/jats:italic> = 44.4 \u00e5. Initial phases were determined by the method of molecular replacement using the oxidized form of the rubredoxin from the mesophilic eubacterium, <jats:italic>Clostridium pasteurianum<\/jats:italic>, as a starting model. The oxidized and reduced models of <jats:italic>P. furiosus<\/jats:italic> rubredoxin each contain 414 nonhydrogen protein atoms comprising 53 residues. The model of the oxidized form contains 61 solvent H<jats:sub>2<\/jats:sub>O oxygen atoms and has been refined with X\u2010PLOR and TNT to a final <jats:italic>R<\/jats:italic> = 0.178 with root mean square (rms) deviations from ideality in bond distances and bond angles of 0.014 \u00e5 and 2.06\u00b0, respectively. The model of the reduced form contains 37 solvent H<jats:sub>2<\/jats:sub>O oxygen atoms and has been refined to <jats:italic>R<\/jats:italic> = 0.193 with rms deviations from ideality in bond lengths of 0.012 \u00e5 and in bond angles of 1.95\u00b0. The overall structure of <jats:italic>P. furiosus<\/jats:italic> rubredoxin is similar to the structures of mesophilic rubredoxins, with the exception of a more extensive hydrogen\u2010bonding network in the \u03b2\u2010sheet region and multiple electrostatic interactions (salt bridge, hydrogen bonds) of the Glu 14 side chain with groups on three other residues (the amino\u2010terminal nitrogen of Ala 1; the indole nitrogen of Trp 3; and the amide nitrogen group of Phe 29). The influence of these and other features upon the thermostability of the <jats:italic>P. furiosus<\/jats:italic> protein is discussed.<\/jats:p>","DOI":"10.1002\/pro.5560011111","type":"journal-article","created":{"date-parts":[[2009,2,10]],"date-time":"2009-02-10T18:02:10Z","timestamp":1234288930000},"page":"1494-1507","source":"Crossref","is-referenced-by-count":173,"title":["X\u2010ray crystal structures of the oxidized and reduced forms of the rubredoxin from the marine hyperthermophilic archaebacterium pyrococcus furiosus"],"prefix":"10.1002","volume":"1","author":[{"given":"Michael W.","family":"Day","sequence":"first","affiliation":[]},{"given":"Barbara T.","family":"Hsu","sequence":"additional","affiliation":[]},{"given":"Leemor","family":"Joshua\u2010Tor","sequence":"additional","affiliation":[]},{"given":"Jae\u2010Bum","family":"Park","sequence":"additional","affiliation":[]},{"given":"Zhi Hao","family":"Zhou","sequence":"additional","affiliation":[]},{"given":"Michael W. 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