2j7a: Difference between revisions

Revision as of 05:43, 28 July 2008

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File:2j7a.png

Template:STRUCTURE 2j7a

CRYSTAL STRUCTURE OF CYTOCHROME C NITRITE REDUCTASE NRFHA COMPLEX FROM DESULFOVIBRIO VULGARISCRYSTAL STRUCTURE OF CYTOCHROME C NITRITE REDUCTASE NRFHA COMPLEX FROM DESULFOVIBRIO VULGARIS

Template:ABSTRACT PUBMED 17139260

About this StructureAbout this Structure

2J7A is a Protein complex structure of sequences from Desulfovibrio vulgaris. Full crystallographic information is available from OCA.

ReferenceReference

X-ray structure of the membrane-bound cytochrome c quinol dehydrogenase NrfH reveals novel haem coordination., Rodrigues ML, Oliveira TF, Pereira IA, Archer M, EMBO J. 2006 Dec 13;25(24):5951-60. Epub 2006 Nov 30. PMID:17139260

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OCA

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 {{STRUCTURE_2j7a|  PDB=2j7a  |  SCENE=  }}
-'''CRYSTAL STRUCTURE OF CYTOCHROME C NITRITE REDUCTASE NRFHA COMPLEX FROM DESULFOVIBRIO VULGARIS'''
+===CRYSTAL STRUCTURE OF CYTOCHROME C NITRITE REDUCTASE NRFHA COMPLEX FROM DESULFOVIBRIO VULGARIS===
-==Overview==
+<!--
-Oxidation of membrane-bound quinol molecules is a central step in the respiratory electron transport chains used by biological cells to generate ATP by oxidative phosphorylation. A novel family of cytochrome c quinol dehydrogenases that play an important role in bacterial respiratory chains was recognised in recent years. Here, we describe the first structure of a cytochrome from this family, NrfH from Desulfovibrio vulgaris, which forms a stable complex with its electron partner, the cytochrome c nitrite reductase NrfA. One NrfH molecule interacts with one NrfA dimer in an asymmetrical manner, forming a large membrane-bound complex with an overall alpha(4)beta(2) quaternary arrangement. The menaquinol-interacting NrfH haem is pentacoordinated, bound by a methionine from the CXXCHXM sequence, with an aspartate residue occupying the distal position. The NrfH haem that transfers electrons to NrfA has a lysine residue from the closest NrfA molecule as distal ligand. A likely menaquinol binding site, containing several conserved and essential residues, is identified.
+The line below this paragraph, {{ABSTRACT_PUBMED_17139260}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 17139260 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_17139260}}
 ==About this Structure==
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 [[Category: Oxidoreductase]]
 [[Category: Quinol dehydrogenase]]
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