2j7a: Difference between revisions
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|PDB= 2j7a |SIZE=350|CAPTION= <scene name='initialview01'>2j7a</scene>, resolution 2.30Å | |PDB= 2j7a |SIZE=350|CAPTION= <scene name='initialview01'>2j7a</scene>, resolution 2.30Å | ||
|SITE= <scene name='pdbsite=AC1:Act+Binding+Site+For+Chain+O'>AC1</scene> | |SITE= <scene name='pdbsite=AC1:Act+Binding+Site+For+Chain+O'>AC1</scene> | ||
|LIGAND= <scene name='pdbligand= | |LIGAND= <scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=LMT:DODECYL-BETA-D-MALTOSIDE'>LMT</scene> | ||
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY= | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2j7a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2j7a OCA], [http://www.ebi.ac.uk/pdbsum/2j7a PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2j7a RCSB]</span> | |||
}} | }} | ||
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[[Category: Pereira, I A.C.]] | [[Category: Pereira, I A.C.]] | ||
[[Category: Rodrigues, M L.]] | [[Category: Rodrigues, M L.]] | ||
[[Category: cytochrome c nitrite reductase]] | [[Category: cytochrome c nitrite reductase]] | ||
[[Category: membrane complex]] | [[Category: membrane complex]] | ||
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[[Category: quinol dehydrogenase]] | [[Category: quinol dehydrogenase]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 03:54:00 2008'' | ||
Revision as of 03:54, 31 March 2008
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| , resolution 2.30Å | |||||||
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| Ligands: | , , , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CRYSTAL STRUCTURE OF CYTOCHROME C NITRITE REDUCTASE NRFHA COMPLEX FROM DESULFOVIBRIO VULGARIS
OverviewOverview
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.
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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