標題: Crystal structure of rubredoxin from Desulfovibrio gigas to ultra-high 0.68 angstrom resolution
作者: Chen, Chun-Jung
Lin, Yi-Hung
Huang, Yen-Chieh
Liu, Ming-Yih
生物科技學系
Department of Biological Science and Technology
關鍵字: rubredoxin;Desulfovibrio gigas;redox;crystal structure;ultra-high resolution;multiple conformations
公開日期: 13-Oct-2006
摘要: Rubredoxin (D.g. Rd) is a small non-heme iron-sulfur protein shown to function as a redox coupling protein from the sulfate reducing bacteria Desulfovibrio gigas. The protein is generally purified from anaerobic bacteria in which it is thought to be involved in electron transfer or exchange processes. Rd transfers an electron to oxygen to form water as part of a unique electron transfer chain, composed by NADH:rubredoxin oxidoreductase (NRO), rubredoxin and rubredoxin: oxygen oxidoreductase (ROO) in D.g. The crystal structure of D.g. Rd has been determined by means of both a Fe single-wavelength anomalous dispersion (SAD) signal and the direct method, and refined to an ultra-high 0.68 angstrom resolution, using X-ray from a synchrotron. Rd contains one iron atom bound in a tetrahedral coordination by the sulfur atoms of four cysteinyl residues. Hydrophobic and it pi-pi interactions maintain the internal Rd folding. Multiple conformations of the iron-sulfur cluster and amino acid residues are observed and indicate its unique mechanism of electron transfer. Several hydrogen bonds, including N-H(...)SG of the iron-sulfur, are revealed clearly in maps of electron density. Abundant waters bound to C-O peptides of residues Val8, Cys9, Gly10, Ala38, and Gly43, which may be involved in electron transfer. This ultra-high-resolution structure allows us to study in great detail the relationship between structure and function of rubredoxin, such as salt bridges, hydrogen bonds, water structures, cysteine ligands, iron-sulfur. cluster, and distributions of electron density among activity sites. For the first time, this information will provide a clear role for this protein in a strict anaerobic bacterium. (c) 2006 Elsevier Inc. All rights reserved.
URI: http://dx.doi.org/10.1016/j.bbrc.2006.07.205
http://hdl.handle.net/11536/11676
ISSN: 0006-291X
DOI: 10.1016/j.bbrc.2006.07.205
期刊: BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
Volume: 349
Issue: 1
起始頁: 79
結束頁: 90
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