1gws: Difference between revisions

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<StructureSection load='1gws' size='340' side='right'caption='[[1gws]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
<StructureSection load='1gws' size='340' side='right'caption='[[1gws]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1gws]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Desulfovibrio_vulgaris Desulfovibrio vulgaris]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GWS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1GWS FirstGlance]. <br>
<table><tr><td colspan='2'>[[1gws]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Desulfovibrio_vulgaris_str._Hildenborough Desulfovibrio vulgaris str. Hildenborough]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GWS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1GWS FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HEC:HEME+C'>HEC</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1h29|1h29]]</div></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HEC:HEME+C'>HEC</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1gws FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gws OCA], [https://pdbe.org/1gws PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1gws RCSB], [https://www.ebi.ac.uk/pdbsum/1gws PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1gws ProSAT]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1gws FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gws OCA], [https://pdbe.org/1gws PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1gws RCSB], [https://www.ebi.ac.uk/pdbsum/1gws PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1gws ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/HMWC_DESVH HMWC_DESVH]] HMWC (high-molecular-weight cytochrome c), ORF2, ORF3, ORF4, ORF5 and ORF6 in the HMC operon form a transmembrane protein complex that allows electron flow from the periplasmic hydrogenase to the cytoplasmic enzymes that catalyze reduction of sulfates.  
[https://www.uniprot.org/uniprot/HMWC_DESVH HMWC_DESVH] HMWC (high-molecular-weight cytochrome c), ORF2, ORF3, ORF4, ORF5 and ORF6 in the HMC operon form a transmembrane protein complex that allows electron flow from the periplasmic hydrogenase to the cytoplasmic enzymes that catalyze reduction of sulfates.
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1gws ConSurf].
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1gws ConSurf].
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<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.
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<ref>PMID:12467575</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1gws" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Cytochrome C 3D structures|Cytochrome C 3D structures]]
*[[Cytochrome C 3D structures|Cytochrome C 3D structures]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Desulfovibrio vulgaris]]
[[Category: Desulfovibrio vulgaris str. Hildenborough]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Bruschi, M]]
[[Category: Bruschi M]]
[[Category: Czjzek, M]]
[[Category: Czjzek M]]
[[Category: Haser, R]]
[[Category: Haser R]]
[[Category: Electron transport]]
[[Category: Heme]]
[[Category: Multiheme cytochrome]]
[[Category: Periplasmic]]
[[Category: Sulfate reducing bacteria]]

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