1up9: Difference between revisions
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[[Image:1up9. | [[Image:1up9.jpg|left|200px]]<br /><applet load="1up9" size="450" color="white" frame="true" align="right" spinBox="true" | ||
<applet load="1up9" size="450" color="white" frame="true" align="right" spinBox="true" | |||
caption="1up9, resolution 1.35Å" /> | caption="1up9, resolution 1.35Å" /> | ||
'''REDUCED STRUCTURE OF CYTOCHROME C3 FROM DESULFOVIBRIO DESULFURICANS ATCC 27774 AT PH 7.6'''<br /> | '''REDUCED STRUCTURE OF CYTOCHROME C3 FROM DESULFOVIBRIO DESULFURICANS ATCC 27774 AT PH 7.6'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
1UP9 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 SO4 and HEC as [http://en.wikipedia.org/wiki/ligands ligands]. | 1UP9 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 SO4 and HEC as [http://en.wikipedia.org/wiki/ligands ligands]. Known structural/functional Site: <scene name='pdbsite=AC1:So4 Binding Site For Chain A205'>AC1</scene>. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1UP9 OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: tetraheme cytochrome c]] | [[Category: tetraheme cytochrome c]] | ||
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Dec 18 18:06:03 2007'' | ||
Revision as of 18:56, 18 December 2007
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REDUCED 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
1UP9 is a Single protein structure of sequence from Desulfovibrio desulfuricans with SO4 and HEC as ligands. Known structural/functional Site: . 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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