1gws: Difference between revisions
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|PDB= 1gws |SIZE=350|CAPTION= <scene name='initialview01'>1gws</scene>, resolution 2.40Å | |PDB= 1gws |SIZE=350|CAPTION= <scene name='initialview01'>1gws</scene>, resolution 2.40Å | ||
|SITE= <scene name='pdbsite=AC1:Hec+Binding+Site+For+Residue+A+616'>AC1</scene> | |SITE= <scene name='pdbsite=AC1:Hec+Binding+Site+For+Residue+A+616'>AC1</scene> | ||
|LIGAND= <scene name='pdbligand= | |LIGAND= <scene name='pdbligand=HEC:HEME+C'>HEC</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene> | ||
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY= | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1gws FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gws OCA], [http://www.ebi.ac.uk/pdbsum/1gws PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1gws RCSB]</span> | |||
}} | }} | ||
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[[Category: Czjzek, M.]] | [[Category: Czjzek, M.]] | ||
[[Category: Haser, R.]] | [[Category: Haser, R.]] | ||
[[Category: electron transport]] | [[Category: electron transport]] | ||
[[Category: heme]] | [[Category: heme]] | ||
[[Category: multiheme cytochrome]] | [[Category: multiheme cytochrome]] | ||
[[Category: periplasmic | [[Category: periplasmic,repeat]] | ||
[[Category: signal]] | [[Category: signal]] | ||
[[Category: sulfate reducing bacteria]] | [[Category: sulfate reducing bacteria]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:52:58 2008'' |
Revision as of 20:53, 30 March 2008
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, resolution 2.40Å | |||||||
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Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
Coordinates: | save as pdb, mmCIF, xml |
HEXADECAHEME HIGH MOLECULAR WEIGHT CYTOCHROME HMC FROM DESULFOVIBRIO VULGARIS HILDENBOROUGH
OverviewOverview
Sulfate-reducing bacteria contain a variety of multi-heme c-type cytochromes. The cytochrome of highest molecular weight (Hmc) contains 16 heme groups and is part of a transmembrane complex involved in the sulfate respiration pathway. We present the 2.42 A resolution crystal structure of the Desulfovibrio vulgaris Hildenborough cytochrome Hmc and a structural model of the complex with its physiological electron transfer partner, cytochrome c(3), obtained by NMR restrained soft-docking calculations. The Hmc is composed of three domains, which exist independently in different sulfate-reducing species, namely cytochrome c(3), cytochrome c(7), and Hcc. The complex involves the last heme at the C-terminal region of the V-shaped Hmc and heme 4 of cytochrome c(3), and represents an example for specific cytochrome-cytochrome interaction.
About this StructureAbout this Structure
1GWS is a Single protein structure of sequence from Desulfovibrio vulgaris. Full crystallographic information is available from OCA.
ReferenceReference
The crystal structure of the hexadeca-heme cytochrome Hmc and a structural model of its complex with cytochrome c(3)., Czjzek M, ElAntak L, Zamboni V, Morelli X, Dolla A, Guerlesquin F, Bruschi M, Structure. 2002 Dec;10(12):1677-86. PMID:12467575
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