1upd: Difference between revisions
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==Overview== | ==Overview== | ||
The tetraheme cytochrome c3 is a small metalloprotein with ca. 13,000 Da, found in sulfate-reducing bacteria, which is believed to act as a partner, of hydrogenase. The three-dimensional structure of the oxidized and, reduced forms of cytochrome c3 from Desulfovibrio desulfuricans ATCC 27774, at pH 7.6 were determined using high-resolution X-ray crystallography and, were compared with the previously determined oxidized form at pH 4.0., Theoretical calculations were performed with both structures, using, continuum electrostatic calculations and Monte Carlo sampling of, protonation and redox states, in order to understand the molecular basis, of the redox-Bohr and cooperativity effects related to the coupled, transfer of electrons and protons. We were able to identify groups that, showed ... | The tetraheme cytochrome c3 is a small metalloprotein with ca. 13,000 Da, found in sulfate-reducing bacteria, which is believed to act as a partner, of hydrogenase. The three-dimensional structure of the oxidized and, reduced forms of cytochrome c3 from Desulfovibrio desulfuricans ATCC 27774, at pH 7.6 were determined using high-resolution X-ray crystallography and, were compared with the previously determined oxidized form at pH 4.0., Theoretical calculations were performed with both structures, using, continuum electrostatic calculations and Monte Carlo sampling of, protonation and redox states, in order to understand the molecular basis, of the redox-Bohr and cooperativity effects related to the coupled, transfer of electrons and protons. We were able to identify groups that, showed redox-linked conformational changes. In particular, Glu61, His76, and propionate D of heme II showed important contributions to the, redox-cooperativity, whereas His76, propionate A of heme I, and propionate, D of heme IV were the key residues for the redox-Bohr effect. Upon, reduction, an important movement of the backbone region surrounding hemes, I and II was also identified, that, together with a few redox-linked, conformational changes in side-chain residues, results in a significant, decrease in the solvent accessibility of hemes I and II. | ||
==About this Structure== | ==About this Structure== | ||
1UPD is a | 1UPD is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Desulfovibrio_desulfuricans Desulfovibrio desulfuricans] with HEC as [http://en.wikipedia.org/wiki/ligand ligand]. Structure known Active Site: AC1. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1UPD OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: tetraheme cytochrome c]] | [[Category: tetraheme cytochrome c]] | ||
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Revision as of 15:33, 5 November 2007
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OXIDIZED STRUCTURE OF CYTOCHROME C3 FROM DESULFOVIBRIO DESULFURICANS ATCC 27774 AT PH 7.6
OverviewOverview
The tetraheme cytochrome c3 is a small metalloprotein with ca. 13,000 Da, found in sulfate-reducing bacteria, which is believed to act as a partner, of hydrogenase. The three-dimensional structure of the oxidized and, reduced forms of cytochrome c3 from Desulfovibrio desulfuricans ATCC 27774, at pH 7.6 were determined using high-resolution X-ray crystallography and, were compared with the previously determined oxidized form at pH 4.0., Theoretical calculations were performed with both structures, using, continuum electrostatic calculations and Monte Carlo sampling of, protonation and redox states, in order to understand the molecular basis, of the redox-Bohr and cooperativity effects related to the coupled, transfer of electrons and protons. We were able to identify groups that, showed redox-linked conformational changes. In particular, Glu61, His76, and propionate D of heme II showed important contributions to the, redox-cooperativity, whereas His76, propionate A of heme I, and propionate, D of heme IV were the key residues for the redox-Bohr effect. Upon, reduction, an important movement of the backbone region surrounding hemes, I and II was also identified, that, together with a few redox-linked, conformational changes in side-chain residues, results in a significant, decrease in the solvent accessibility of hemes I and II.
About this StructureAbout this Structure
1UPD is a Single protein structure of sequence from Desulfovibrio desulfuricans with HEC as ligand. Structure known Active Site: AC1. Full crystallographic information is available from OCA.
ReferenceReference
Molecular basis for redox-Bohr and cooperative effects in cytochrome c3 from Desulfovibrio desulfuricans ATCC 27774: crystallographic and modeling studies of oxidized and reduced high-resolution structures at pH 7.6., Bento I, Matias PM, Baptista AM, da Costa PN, van Dongen WM, Saraiva LM, Schneider TR, Soares CM, Carrondo MA, Proteins. 2004 Jan 1;54(1):135-52. PMID:14705030
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