1gws: Difference between revisions

Revision as of 13:54, 21 February 2008

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 with and as ligands. Known structural/functional Site: . 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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 ==Overview==
-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.
+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 Structure==
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 [[Category: sulfate reducing bacteria]]
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