1gn9
From Proteopedia
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'''HYBRID CLUSTER PROTEIN FROM DESULFOVIBRIO DESULFURICANS ATCC 27774 X-RAY STRUCTURE AT 2.6A RESOLUTION USING SYNCHROTRON RADIATION AT A WAVELENGTH OF 1.722A''' | '''HYBRID CLUSTER PROTEIN FROM DESULFOVIBRIO DESULFURICANS ATCC 27774 X-RAY STRUCTURE AT 2.6A RESOLUTION USING SYNCHROTRON RADIATION AT A WAVELENGTH OF 1.722A''' | ||
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[[Category: Teixeira, M.]] | [[Category: Teixeira, M.]] | ||
[[Category: Xavier, A.]] | [[Category: Xavier, A.]] | ||
- | [[Category: | + | [[Category: Anaerobic desulfovibrio desulfurican]] |
- | [[Category: | + | [[Category: Hybrid cluster protein]] |
- | [[Category: | + | [[Category: Iron anomalous]] |
- | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 17:46:32 2008'' | |
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + |
Revision as of 14:46, 2 May 2008
HYBRID CLUSTER PROTEIN FROM DESULFOVIBRIO DESULFURICANS ATCC 27774 X-RAY STRUCTURE AT 2.6A RESOLUTION USING SYNCHROTRON RADIATION AT A WAVELENGTH OF 1.722A
Overview
The structures of the hybrid cluster proteins (HCPs) from the sulfate-reducing bacteria Desulfovibrio desulfuricans (ATCC 27774) and Desulfovibrio vulgaris (Hildenborough) have been elucidated at a resolution of 1.25 A using X-ray synchrotron radiation techniques. In the case of the D. desulfuricans protein, protein isolation, purification, crystallization and X-ray data collection were carried out under strict anaerobic conditions, whereas for the D. vulgaris protein the conditions were aerobic. However, both structures are essentially the same, comprising three domains and two iron-sulfur centres. One of these centres situated near the exterior of the molecules in domain 1 is a cubane [4Fe-4S] cluster, whereas the other, located at the interface of the three domains, contains the unusual four-iron cluster initially found in the D. vulgaris protein. Details of the structures and the associated EPR spectroscopy of the D. desulfuricans protein are reported herein. These structures show that the nature of the hybrid cluster, containing both oxygen and sulfur bridges, is independent of the presence of oxygen in the isolation and crystallization procedure and also does not vary significantly with changes in the oxidation state. The structures and amino acid sequences of the HCP are compared with the recently elucidated structure of the catalytic subunit of a carbon monoxide dehydrogenase from Carboxydothermus hydrogenoformans and related dehydrogenases. Electronic supplementary material to this paper can be obtained by using the Springer Link server located at http://dx.doi.org/10.1007/s00775-001-0326-y.
About this Structure
1GN9 is a Single protein structure of sequence from Desulfovibrio desulfuricans. Full crystallographic information is available from OCA.
Reference
Hybrid cluster proteins (HCPs) from Desulfovibrio desulfuricans ATCC 27774 and Desulfovibrio vulgaris (Hildenborough): X-ray structures at 1.25 A resolution using synchrotron radiation., Macedo S, Mitchell EP, Romao CV, Cooper SJ, Coelho R, Liu MY, Xavier AV, LeGall J, Bailey S, Garner DC, Hagen WR, Teixeira M, Carrondo MA, Lindley P, J Biol Inorg Chem. 2002 Apr;7(4-5):514-25. Epub 2002 Jan 23. PMID:11941509 Page seeded by OCA on Fri May 2 17:46:32 2008
Categories: Desulfovibrio desulfuricans | Single protein | Bailey, S. | Carrondo, M. | Coelho, R. | Cooper, S. | Garner, C. | Hagen, W. | Legall, J. | Lindley, P. | Liu, M. | Macedo, S. | Mitchell, E. | Romao, C. | Teixeira, M. | Xavier, A. | Anaerobic desulfovibrio desulfurican | Hybrid cluster protein | Iron anomalous