X-ray crystal structures of the oxidized and reduced forms of the rubredoxin from the marine hyperthermophilic archaebacterium pyrococcus furiosus
| Autor: | Zhi Hao Zhou, Leemor Joshua-Tor, Douglas C. Rees, Barbara T. Hsu, Jae-Bum Park, Michael W. W. Adams, Michael W. Day |
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| Rok vydání: | 1992 |
| Předmět: |
Models
Molecular Hot Temperature Protein Conformation Molecular Sequence Data Crystal structure Biochemistry Protein Structure Secondary Drug Stability X-Ray Diffraction Rubredoxin Molecular replacement Amino Acid Sequence Molecular Biology Thermostability Sequence Homology Amino Acid biology Hydrogen bond Chemistry Rubredoxins Hydrogen Bonding biology.organism_classification Archaea Bond length Crystallography Molecular geometry Pyrococcus furiosus Thermodynamics Crystallization Oxidation-Reduction Mathematics Research Article |
| Zdroj: | Protein Science. 1:1494-1507 |
| ISSN: | 1469-896X 0961-8368 |
| DOI: | 10.1002/pro.5560011111 |
| Popis: | The structures of the oxidized and reduced forms of the rubredoxin from the archaebacterium, Pyrococcus furiosus, an organism that grows optimally at 100 degrees C, have been determined by X-ray crystallography to a resolution of 1.8 A. Crystals of this rubredoxin grow in space group P2(1)2(1)2(1) with room temperature cell dimensions a = 34.6 A, b = 35.5 A, and c = 44.4 A. 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 H2O 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 A and 2.06 degrees, 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 A and in bond angles of 1.95 degrees. 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 beta-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. |
| Databáze: | OpenAIRE |
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