1ofw: Difference between revisions
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[[Image:1ofw.jpg|left|200px]]<br /><applet load="1ofw" size=" | [[Image:1ofw.jpg|left|200px]]<br /><applet load="1ofw" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1ofw, resolution 1.5Å" /> | caption="1ofw, resolution 1.5Å" /> | ||
'''THREE DIMENSIONAL STRUCTURE OF THE OXIDIZED FORM OF NINE HEME CYTOCHROME C AT PH 7.5'''<br /> | '''THREE DIMENSIONAL STRUCTURE OF THE OXIDIZED FORM OF NINE HEME CYTOCHROME C AT PH 7.5'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
1OFW 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 ACT, HEC and GOL as [http://en.wikipedia.org/wiki/ligands ligands]. Known structural/functional Site: <scene name='pdbsite=AC1:Gol Binding Site For Chain B'>AC1</scene>. Full crystallographic information is available from [http:// | 1OFW 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 <scene name='pdbligand=ACT:'>ACT</scene>, <scene name='pdbligand=HEC:'>HEC</scene> and <scene name='pdbligand=GOL:'>GOL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Known structural/functional Site: <scene name='pdbsite=AC1:Gol+Binding+Site+For+Chain+B'>AC1</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OFW OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: multiheme cytochrome c]] | [[Category: multiheme cytochrome c]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb 3 09:57:35 2008'' | ||
Revision as of 10:57, 3 February 2008
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THREE DIMENSIONAL STRUCTURE OF THE OXIDIZED FORM OF NINE HEME CYTOCHROME C AT PH 7.5
OverviewOverview
The nine-heme cytochrome c is a monomeric multiheme cytochrome found in, Desulfovibrio desulfuricans ATCC 27774. The polypeptide chain comprises, 296 residues and wraps around nine hemes of type c. It is believed to take, part in the periplasmic assembly of proteins involved in the mechanism of, hydrogen cycling, receiving electrons from the tetraheme cytochrome c3., With the purpose of understanding the molecular basis of electron transfer, processes in this cytochrome, we have determined the crystal structures of, its oxidized and reduced forms at pH 7.5 and performed theoretical, calculations of the binding equilibrium of protons and electrons in these, structures. This integrated study allowed us to observe that the reduction, process induced relevant conformational changes in several residues, as, well as protonation changes in some protonatable residues. In particular, the surroundings of hemes I and IV constitute two areas of special, interest. In addition, we were able to ascertain the groups involved in, the redox-Bohr effect present in this cytochrome and the conformational, changes that may underlie the redox-cooperativity effects on different, hemes. Furthermore, the thermodynamic simulations provide evidence that, the N- and C-terminal domains function in an independent manner, with the, hemes belonging to the N-terminal domain showing, in general, a lower, redox potential than those found in the C-terminal domain. In this way, electrons captured by the N-terminal domain could easily flow to the, C-terminal domain, allowing the former to capture more electrons. A, notable exception is heme IX, which has low redox potential and could, serve as the exit path for electrons toward other proteins in the electron, transfer pathway.
About this StructureAbout this Structure
1OFW is a Single protein structure of sequence from Desulfovibrio desulfuricans with , and as ligands. Known structural/functional Site: . Full crystallographic information is available from OCA.
ReferenceReference
Redox-Bohr and other cooperativity effects in the nine-heme cytochrome C from Desulfovibrio desulfuricans ATCC 27774: crystallographic and modeling studies., Bento I, Teixeira VH, Baptista AM, Soares CM, Matias PM, Carrondo MA, J Biol Chem. 2003 Sep 19;278(38):36455-69. Epub 2003 May 15. PMID:12750363
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