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X-ray Crystal Structures of the Oxidized and Reduced forms of the Rubredoxin from the Marine Hyperthermophilic Archaebacterium Pyrococcus furiosus

Day, Michael W. and Hsu, Barbara T. and Joshua-Tor, Leemor and Park, Jae-Bum and Zhou, Zhi Hao and Adams, Michael W. W. and Rees, Douglas C. (1992) X-ray Crystal Structures of the Oxidized and Reduced forms of the Rubredoxin from the Marine Hyperthermophilic Archaebacterium Pyrococcus furiosus. Protein Science, 1 (11). pp. 1494-1507. ISSN 0961-8368. PMCID PMC2142115. http://resolver.caltech.edu/CaltechAUTHORS:20150209-101936300

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Abstract

The structures of the oxidized and reduced forms of the rubredoxin from the archaebacterium, Pyrococcus furiosus, an organism that grows optimally at 100 °C, have been determined by X-ray crystallography to a resolution of 1.8 å. Crystals of this rubredoxin grow in space group P2_12_12_1 with room temperature cell dimensions a = 34.6 å, b = 35.5 å, and c = 44.4 å. Initial phases were determined by the method of molecular replacement using the oxidized form of the rubredoxin from the mesophilic eubacterium, Clostridium pasteurianum, as a starting model. The oxidized and reduced models of P. furiosus rubredoxin each contain 414 nonhydrogen protein atoms comprising 53 residues. The model of the oxidized form contains 61 solvent H_2O oxygen atoms and has been refined with X-PLOR and TNT to a final R = 0.178 with root mean square (rms) deviations from ideality in bond distances and bond angles of 0.014 å and 2.06°, respectively. The model of the reduced form contains 37 solvent H2O oxygen atoms and has been refined to R = 0.193 with rms deviations from ideality in bond lengths of 0.012 å and in bond angles of 1.95°. The overall structure of P. furiosus rubredoxin is similar to the structures of mesophilic rubredoxins, with the exception of a more extensive hydrogen-bonding network in the β-sheet region and multiple electrostatic interactions (salt bridge, hydrogen bonds) of the Glu 14 side chain with groups on three other residues (the amino-terminal 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 P. furiosus protein is discussed.


Item Type:Article
Related URLs:
URLURL TypeDescription
http://dx.doi.org/10.1002/pro.5560011111DOIArticle
http://onlinelibrary.wiley.com/doi/10.1002/pro.5560011111/abstractPublisherArticle
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2142115/PubMed CentralArticle
Contact Email Address:phoebe@caltech.edu
Additional Information:© 1992 The Protein Society. Received April 29, 1992; Revised manuscript received June 9, 1992. We thank A.J. Chirino for his advice and assistance throughout the course of this research. This work was supported by grants from the National Science Foundation DMB-9118689 (D.C.R), and BCS-9011583 (M.W.W.A.), the Office of Naval Research N00014-90-J-1894 (M.W.W.A.), and by a National Science Foundation Training Group Award to the Center for Metalloenzyme Studies of the University of Georgia DIR-9014281. We also acknowledge the Department of Education (M.W.D.) and a Weizmann postdoctoral fellowship (L.J.) for support.
Funders:
Funding AgencyGrant Number
NSFDMB-9118689
NSFBCS-9011583
Office of Naval Research (ONR)N00014-90-J-1894
NSFDIR-9014281
Department of EducationUNSPECIFIED
Weizmann Postdoctoral Fellowship (Caltech)UNSPECIFIED
Subject Keywords:electron transfer proteins; protein stability; protein structure; rubredoxin; thermostability
PubMed Central ID:PMC2142115
Record Number:CaltechAUTHORS:20150209-101936300
Persistent URL:http://resolver.caltech.edu/CaltechAUTHORS:20150209-101936300
Official Citation:Day, M. W., Hsu, B. T., Joshua-Tor, L., Park, J.-B., Zhou, Z. H., Adams, M. W. W. and Rees, D. C. (1992), X-ray crystal structures of the oxidized and reduced forms of the rubredoxin from the marine hyperthermophilic archaebacterium pyrococcus furiosus. Protein Science, 1: 1494–1507. doi: 10.1002/pro.5560011111
Usage Policy:No commercial reproduction, distribution, display or performance rights in this work are provided.
ID Code:54536
Collection:CaltechAUTHORS
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Deposited On:10 Feb 2015 05:34
Last Modified:10 Feb 2015 05:34

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