1upd
From Proteopedia
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| - | [[Image:1upd.gif|left|200px]] | + | [[Image:1upd.gif|left|200px]] |
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| - | '''OXIDIZED STRUCTURE OF CYTOCHROME C3 FROM DESULFOVIBRIO DESULFURICANS ATCC 27774 AT PH 7.6''' | + | {{Structure |
| + | |PDB= 1upd |SIZE=350|CAPTION= <scene name='initialview01'>1upd</scene>, resolution 1.40Å | ||
| + | |SITE= <scene name='pdbsite=AC1:Hec+Binding+Site+For+Chain+A'>AC1</scene> | ||
| + | |LIGAND= <scene name='pdbligand=HEC:HEME C'>HEC</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''OXIDIZED STRUCTURE OF CYTOCHROME C3 FROM DESULFOVIBRIO DESULFURICANS ATCC 27774 AT PH 7.6''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1UPD is a [ | + | 1UPD is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Desulfovibrio_desulfuricans Desulfovibrio desulfuricans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UPD OCA]. |
==Reference== | ==Reference== | ||
| - | 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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/14705030 14705030] |
[[Category: Desulfovibrio desulfuricans]] | [[Category: Desulfovibrio desulfuricans]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: tetraheme cytochrome c]] | [[Category: tetraheme cytochrome c]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:35:05 2008'' |
Revision as of 12:35, 20 March 2008
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| , resolution 1.40Å | |||||||
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
OXIDIZED STRUCTURE OF CYTOCHROME C3 FROM DESULFOVIBRIO DESULFURICANS ATCC 27774 AT PH 7.6
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 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
1UPD is a Single protein structure of sequence from Desulfovibrio desulfuricans. Full crystallographic information is available from OCA.
Reference
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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