Crystallization and preliminary X-ray studies of ferredoxin-NAD(P){sup +} reductase from Chlorobium tepidum
- Department of Life Sciences, University of Tokyo, Komaba, Meguro-ku, Tokyo 153-8902 (Japan)
- Graduate School of Natural Science and Technology, Kanazawa University, Kakuma, Kanazawa 920-1192 (Japan)
Ferredoxin-NAD(P){sup +} reductase from C. tepidum has been overexpressed in E. coli, purified and crystallized. Diffraction data were collected to 2.4 Å resolution. Ferredoxin-NAD(P){sup +} reductase (FNR) is a key enzyme that catalyzes the photoreduction of NAD(P){sup +} to generate NAD(P)H during the final step of the photosynthetic electron-transport chain. FNR from the green sulfur bacterium Chlorobium tepidum is a homodimeric enzyme with a molecular weight of 90 kDa; it shares a high level of amino-acid sequence identity to thioredoxin reductase rather than to conventional plant-type FNRs. In order to understand the structural basis of the ferredoxin-dependency of this unique photosynthetic FNR, C. tepidum FNR has been heterologously expressed, purified and crystallized in two forms. Form I crystals belong to space group C222{sub 1} and contain one dimer in the asymmetric unit, while form II crystals belong to space group P4{sub 1}22 or P4{sub 3}22. Diffraction data were collected from a form I crystal to 2.4 Å resolution on the synchrotron-radiation beamline NW12 at the Photon Factory.
- OSTI ID:
- 22360484
- Journal Information:
- Acta Crystallographica. Section F, Vol. 64, Issue Pt 3; Other Information: PMCID: PMC2374157; PMID: 18323604; PUBLISHER-ID: hc5044; OAI: oai:pubmedcentral.nih.gov:2374157; Copyright (c) International Union of Crystallography 2008; Country of input: International Atomic Energy Agency (IAEA); ISSN 1744-3091
- Country of Publication:
- United Kingdom
- Language:
- English
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