1gn9

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[[Image:1gn9.gif|left|200px]]
[[Image:1gn9.gif|left|200px]]
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{{Structure
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|PDB= 1gn9 |SIZE=350|CAPTION= <scene name='initialview01'>1gn9</scene>, resolution 2.60&Aring;
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The line below this paragraph, containing "STRUCTURE_1gn9", creates the "Structure Box" on the page.
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|LIGAND= <scene name='pdbligand=CSS:S-MERCAPTOCYSTEINE'>CSS</scene>, <scene name='pdbligand=FSO:IRON/SULFUR/OXYGEN+HYBRID+CLUSTER'>FSO</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</scene>
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{{STRUCTURE_1gn9| PDB=1gn9 | SCENE= }}
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1gn9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gn9 OCA], [http://www.ebi.ac.uk/pdbsum/1gn9 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1gn9 RCSB]</span>
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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.]]
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[[Category: anaerobic desulfovibrio desulfurican]]
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[[Category: Anaerobic desulfovibrio desulfurican]]
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[[Category: hybrid cluster protein]]
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[[Category: Hybrid cluster protein]]
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[[Category: iron anomalous]]
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[[Category: Iron anomalous]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 17:46:32 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:47:34 2008''
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Revision as of 14:46, 2 May 2008

Template:STRUCTURE 1gn9

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

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