1gx7

From Proteopedia

(Difference between revisions)

Current revision

Best model of the electron transfer complex between cytochrome c3 and [Fe]-hydrogenase

Structural highlights

1gx7 is a 3 chain structure with sequence from Desulfovibrio vulgaris str. Hildenborough. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	Hybrid , Solution NMR , Theoretical Model, 1 model
Ligands:	, , , ,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

PHFL_NITV2 May be involved in hydrogen uptake for the reduction of sulfate to hydrogen sulfide in an electron transport chain. Cytochrome c3 is likely to be the physiological electron carrier for the enzyme.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

Cytochrome c(3) (M(r) 13000) is a low redox potential cytochrome specific of the anaerobic metabolism in sulfate-reducing bacteria. This tetrahemic cytochrome is an intermediate between the [Fe]-hydrogenase and the cytochrome Hmc in Desulfovibrio vulgaris Hildenborough strain. The present work describes the structural model of the cytochrome c(3)-[Fe]-hydrogenase complex obtained by nuclear magnetic resonance restrained docking. This model connects the distal cluster of the [Fe]-hydrogenase to heme 4 of the cytochrome, the same heme found in the interaction with cytochrome Hmc. This result gives evidence that cytochrome c(3) is an electron shuttle between the periplasmic hydrogenase and the Hmc membrane-bound complex.

The cytochrome c3-[Fe]-hydrogenase electron-transfer complex: structural model by NMR restrained docking.,ElAntak L, Morelli X, Bornet O, Hatchikian C, Czjzek M, Dolla A, Guerlesquin F FEBS Lett. 2003 Jul 31;548(1-3):1-4. PMID:12885397^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ ElAntak L, Morelli X, Bornet O, Hatchikian C, Czjzek M, Dolla A, Guerlesquin F. The cytochrome c3-[Fe]-hydrogenase electron-transfer complex: structural model by NMR restrained docking. FEBS Lett. 2003 Jul 31;548(1-3):1-4. PMID:12885397

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1gx7"

@@ Line 1: / Line 1: @@
-==BEST MODEL OF THE ELECTRON TRANSFER COMPLEX BETWEEN CYTOCHROME C3 AND [FE]-HYDROGENASE==
-<StructureSection load='1gx7' size='340' side='right' caption='[[1gx7]], [[NMR_Ensembles_of_Models | 1 NMR models]]' scene=''>
+==Best model of the electron transfer complex between cytochrome c3 and [Fe]-hydrogenase==
+<StructureSection load='1gx7' size='340' side='right'caption='[[1gx7]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1gx7]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Desulfovibrio_vulgaris Desulfovibrio vulgaris]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GX7 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1GX7 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1gx7]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Desulfovibrio_vulgaris_str._Hildenborough Desulfovibrio vulgaris str. Hildenborough]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GX7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1GX7 FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CMO:CARBON+MONOXIDE'>CMO</scene>, <scene name='pdbligand=CYN:CYANIDE+ION'>CYN</scene>, <scene name='pdbligand=FE2:FE+(II)+ION'>FE2</scene>, <scene name='pdbligand=HEC:HEME+C'>HEC</scene>, <scene name='pdbligand=PDT:1,3-PROPANEDITHIOL'>PDT</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Hybrid , Solution NMR , Theoretical Model, 1 model</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1hfe|1hfe]], [[1a2i|1a2i]], [[1mdv|1mdv]], [[2cth|2cth]], [[2cym|2cym]]</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CMO:CARBON+MONOXIDE'>CMO</scene>, <scene name='pdbligand=CYN:CYANIDE+ION'>CYN</scene>, <scene name='pdbligand=FE2:FE+(II)+ION'>FE2</scene>, <scene name='pdbligand=HEC:HEME+C'>HEC</scene>, <scene name='pdbligand=PDT:1,3-PROPANEDITHIOL'>PDT</scene></td></tr>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Ferredoxin_hydrogenase Ferredoxin hydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.12.7.2 1.12.7.2] </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=1gx7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gx7 OCA], [https://pdbe.org/1gx7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1gx7 RCSB], [https://www.ebi.ac.uk/pdbsum/1gx7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1gx7 ProSAT]</span></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1gx7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gx7 OCA], [http://pdbe.org/1gx7 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1gx7 RCSB], [http://www.ebi.ac.uk/pdbsum/1gx7 PDBsum]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/PHFL_DESVH PHFL_DESVH]] May be involved in hydrogen uptake for the reduction of sulfate to hydrogen sulfide in an electron transport chain. Cytochrome c3 is likely to be the physiological electron carrier for the enzyme. [[http://www.uniprot.org/uniprot/CYC3_DESVH CYC3_DESVH]] Participates in sulfate respiration coupled with phosphorylation by transferring electrons from the enzyme dehydrogenase to ferredoxin. [[http://www.uniprot.org/uniprot/PHFS_DESVH PHFS_DESVH]] May be involved in hydrogen uptake for the reduction of sulfate to hydrogen sulfide in an electron transport chain. Cytochrome c3 is likely to be the physiological electron carrier for the enzyme.
+[https://www.uniprot.org/uniprot/PHFL_NITV2 PHFL_NITV2] May be involved in hydrogen uptake for the reduction of sulfate to hydrogen sulfide in an electron transport chain. Cytochrome c3 is likely to be the physiological electron carrier for the enzyme.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
 Check<jmol>
   <jmolCheckbox>
-    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/gx/1gx7_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/gx/1gx7_consurf.spt"</scriptWhenChecked>
-    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
   </jmolCheckbox>
-</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/chain_selection.php?pdb_ID=2ata 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=1gx7 ConSurf].
 <div style="clear:both"></div>
 <div style="background-color:#fffaf0;">
@@ Line 31: / Line 31: @@
 ==See Also==
-*[[Cytochrome c|Cytochrome c]]
+*[[Cytochrome C 3D structures|Cytochrome C 3D structures]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Desulfovibrio vulgaris]]
+[[Category: Desulfovibrio vulgaris str. Hildenborough]]
-[[Category: Ferredoxin hydrogenase]]
+[[Category: Large Structures]]
-[[Category: Bornet, O]]
+[[Category: Bornet O]]
-[[Category: Czjzek, M]]
+[[Category: Czjzek M]]
-[[Category: Dolla, A]]
+[[Category: Dolla A]]
-[[Category: Elantak, L]]
+[[Category: Elantak L]]
-[[Category: Guerlesquin, F]]
+[[Category: Guerlesquin F]]
-[[Category: Hatchikian, C]]
+[[Category: Hatchikian C]]
-[[Category: Morelli, X]]
+[[Category: Morelli X]]
-[[Category: Electron transfer complex]]
-[[Category: Hydrogenase]]
-[[Category: Iron-sulfur]]
-[[Category: Multiheme cytochrome]]
-[[Category: Oxidoreductase]]
-[[Category: Oxidoreductase electron transport]]
-[[Category: Soft docking]]

1gx7

From Proteopedia

Current revision

Best model of the electron transfer complex between cytochrome c3 and [Fe]-hydrogenase

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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