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Title: Crystallization and preliminary X-ray diffraction studies of a ferredoxin reductase from Rhodopseudomonas palustris CGA009

Abstract

Palustrisredoxin reductase (RPA3782, PuR), a flavin-dependent ferredoxin reductase, is an essential component of the Class I cytochrome P450 systems in Rhodopseudomonas palustris CGA009. Crystals of PuR that diffract to 2.2 Å resolution have been obtained. Palustrisredoxin reductase from Rhodopseudomonas palustris CGA009, a member of the oxygenase-coupled NADH-dependent ferredoxin reductase (ONFR) family, catalyzes electron transfer from NADH to ferredoxins. It is an essential component of the cytochrome P450 systems in R. palustris CGA009, a model organism with diverse metabolic pathways. Here, the crystallization of palustrisredoxin reductase is reported. The crystals belong to the trigonal space group P3{sub 2}21, with unit-cell parameters a = 107.5, b = 107.5, c = 69.9 Å, and diffract to 2.2 Å resolution on a synchrotron source.

Authors:
;  [1]; ;  [2];  [1];  [3]
  1. Laboratory of Structural Biology, School of Medicine, Tsinghua University, Beijing 100084 (China)
  2. Department of Chemistry, University of Oxford, Inorganic Chemistry Laboratory, South Parks Road, Oxford OX1 3QR (United Kingdom)
  3. (IBP), Chinese Academy of Sciences, Beijing 100101 (China)
Publication Date:
OSTI Identifier:
22360334
Resource Type:
Journal Article
Resource Relation:
Journal Name: Acta Crystallographica. Section F; Journal Volume: 63; Journal Issue: Pt 5; Other Information: PMCID: PMC2335014; PMID: 17565187; PUBLISHER-ID: pu5184; OAI: oai:pubmedcentral.nih.gov:2335014; Copyright (c) International Union of Crystallography 2007; Country of input: International Atomic Energy Agency (IAEA)
Country of Publication:
United Kingdom
Language:
English
Subject:
75 CONDENSED MATTER PHYSICS, SUPERCONDUCTIVITY AND SUPERFLUIDITY; CRYSTALLIZATION; CRYSTALS; ELECTRON TRANSFER; OXYGEN; RESOLUTION; SPACE GROUPS; X-RAY DIFFRACTION

Citation Formats

Peng, Ying, Xu, Feng, E-mail: xuf@xtal.tsinghua.edu.cn, Bell, Stephen G., Wong, Luet-Lok, E-mail: xuf@xtal.tsinghua.edu.cn, Rao, Zihe, and National Laboratory of Biomacromolecules, Institute of Biophysics. Crystallization and preliminary X-ray diffraction studies of a ferredoxin reductase from Rhodopseudomonas palustris CGA009. United Kingdom: N. p., 2007. Web. doi:10.1107/S1744309107017411.
Peng, Ying, Xu, Feng, E-mail: xuf@xtal.tsinghua.edu.cn, Bell, Stephen G., Wong, Luet-Lok, E-mail: xuf@xtal.tsinghua.edu.cn, Rao, Zihe, & National Laboratory of Biomacromolecules, Institute of Biophysics. Crystallization and preliminary X-ray diffraction studies of a ferredoxin reductase from Rhodopseudomonas palustris CGA009. United Kingdom. doi:10.1107/S1744309107017411.
Peng, Ying, Xu, Feng, E-mail: xuf@xtal.tsinghua.edu.cn, Bell, Stephen G., Wong, Luet-Lok, E-mail: xuf@xtal.tsinghua.edu.cn, Rao, Zihe, and National Laboratory of Biomacromolecules, Institute of Biophysics. Tue . "Crystallization and preliminary X-ray diffraction studies of a ferredoxin reductase from Rhodopseudomonas palustris CGA009". United Kingdom. doi:10.1107/S1744309107017411.
@article{osti_22360334,
title = {Crystallization and preliminary X-ray diffraction studies of a ferredoxin reductase from Rhodopseudomonas palustris CGA009},
author = {Peng, Ying and Xu, Feng, E-mail: xuf@xtal.tsinghua.edu.cn and Bell, Stephen G. and Wong, Luet-Lok, E-mail: xuf@xtal.tsinghua.edu.cn and Rao, Zihe and National Laboratory of Biomacromolecules, Institute of Biophysics},
abstractNote = {Palustrisredoxin reductase (RPA3782, PuR), a flavin-dependent ferredoxin reductase, is an essential component of the Class I cytochrome P450 systems in Rhodopseudomonas palustris CGA009. Crystals of PuR that diffract to 2.2 Å resolution have been obtained. Palustrisredoxin reductase from Rhodopseudomonas palustris CGA009, a member of the oxygenase-coupled NADH-dependent ferredoxin reductase (ONFR) family, catalyzes electron transfer from NADH to ferredoxins. It is an essential component of the cytochrome P450 systems in R. palustris CGA009, a model organism with diverse metabolic pathways. Here, the crystallization of palustrisredoxin reductase is reported. The crystals belong to the trigonal space group P3{sub 2}21, with unit-cell parameters a = 107.5, b = 107.5, c = 69.9 Å, and diffract to 2.2 Å resolution on a synchrotron source.},
doi = {10.1107/S1744309107017411},
journal = {Acta Crystallographica. Section F},
number = Pt 5,
volume = 63,
place = {United Kingdom},
year = {Tue May 01 00:00:00 EDT 2007},
month = {Tue May 01 00:00:00 EDT 2007}
}
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  • The electron-transfer complex of BphA3, a Rieske-type [2Fe–2S] ferredoxin, and BphA4, a NADH-dependent ferredoxin reductase, was crystallized by the sitting-drop vapour-diffusion method under anaerobic conditions. The electron-transfer complex of BphA3, a Rieske-type [2Fe–2S] ferredoxin, and BphA4, a NADH-dependent ferredoxin reductase, was crystallized using the sitting-drop vapour-diffusion method under anaerobic conditions. The obtained crystals were analyzed by SDS–PAGE, which showed that they contained both BphA3 and BphA4. The crystals belong to space group P2{sub 1}, with unit-cell parameters a = 60.60, b = 173.72, c = 60.98 Å, β = 115.8°, and diffracted to a resolution of 1.9 Å.
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