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==Overview==
==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 ... [[http://ispc.weizmann.ac.il/pmbin/getpm?12467575 (full description)]]
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==
==About this Structure==
1GWS is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Desulfovibrio_vulgaris Desulfovibrio vulgaris]] with HEM and HEC as [[http://en.wikipedia.org/wiki/ligands ligands]]. Structure known Active Site: AC1. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1GWS OCA]].  
1GWS is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Desulfovibrio_vulgaris Desulfovibrio vulgaris] with HEM and HEC as [http://en.wikipedia.org/wiki/ligands ligands]. Structure known Active Site: AC1. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1GWS OCA].  


==Reference==
==Reference==
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[[Category: sulfate reducing bacteria]]
[[Category: sulfate reducing bacteria]]


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Revision as of 13:30, 5 November 2007

File:1gws.gif


1gws, resolution 2.40Å

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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 HEM and HEC as ligands. Structure known Active Site: AC1. 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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