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3cx5

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Revision as of 10:30, 12 August 2020

Structure of complex III with bound cytochrome c in reduced state and definition of a minimal core interface for electron transfer.

Structural highlights

3cx5 is a 23 chain structure with sequence from Lk3 transgenic mice and Saccharomyces cerevisiae. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	, , , , , , , , , , ,
NonStd Res:
Related:	3cxh, 1ezv, 1kb9, 1kyo
Activity:	Ubiquinol--cytochrome-c reductase, with EC number 1.10.2.2
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[QCR6_YEAST] Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex), which is part of the mitochondrial respiratory chain that generates an electrochemical potential coupled to ATP synthesis. The complex couples electron transfer from ubiquinol to cytochrome c. QCR6 may mediate formation of the complex between cytochromes c and c1. [CYB_YEAST] Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex), which is part of the mitochondrial respiratory chain that generates an electrochemical potential coupled to ATP synthesis. The complex couples electron transfer from ubiquinol to cytochrome c. [QCR7_YEAST] Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex), which is part of the mitochondrial respiratory chain that generates an electrochemical potential coupled to ATP synthesis. The complex couples electron transfer from ubiquinol to cytochrome c. QCR7 is involved in redox-linked proton pumping. [QCR9_YEAST] Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex), which is part of the mitochondrial respiratory chain that generates an electrochemical potential coupled to ATP synthesis. The complex couples electron transfer from ubiquinol to cytochrome c. QCR9 is required for formation of a fully functional complex. [CYC1_YEAST] Electron carrier protein. The oxidized form of the cytochrome c heme group can accept an electron from the heme group of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c then transfers this electron to the cytochrome oxidase complex, the final protein carrier in the mitochondrial electron-transport chain. [QCR2_YEAST] Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex), which is part of the mitochondrial respiratory chain that generates an electrochemical potential coupled to ATP synthesis. The complex couples electron transfer from ubiquinol to cytochrome c. QCR2 is required for the assembly of the complex. [QCR8_YEAST] Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex), which is part of the mitochondrial respiratory chain that generates an electrochemical potential coupled to ATP synthesis. The complex couples electron transfer from ubiquinol to cytochrome c. QCR8, together with cytochrome b, binds to ubiquinone. [QCR1_YEAST] Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex), which is part of the mitochondrial respiratory chain that generates an electrochemical potential coupled to ATP synthesis. The complex couples electron transfer from ubiquinol to cytochrome c. COR1 may mediate formation of the complex between cytochromes c and c1. [CY1_YEAST] Heme-containing component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex), which is part of the mitochondrial respiratory chain that generates an electrochemical potential coupled to ATP synthesis. The complex couples electron transfer from ubiquinol to cytochrome c. [UCRI_YEAST] Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex), which is a respiratory chain that generates an electrochemical potential coupled to ATP synthesis. The complex couples electron transfer from ubiquinol to cytochrome c.

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

In cellular respiration, cytochrome c transfers electrons from cytochrome bc(1) complex (complex III) to cytochrome c oxidase by transiently binding to the membrane proteins. Here, we report the structure of isoform-1 cytochrome c bound to cytochrome bc(1) complex at 1.9 A resolution in reduced state. The dimer structure is asymmetric. Monovalent cytochrome c binding is correlated with conformational changes of the Rieske head domain and subunit QCR6p and with a higher number of interfacial water molecules bound to cytochrome c(1). Pronounced hydration and a "mobility mismatch" at the interface with disordered charged residues on the cytochrome c side are favorable for transient binding. Within the hydrophobic interface, a minimal core was identified by comparison with the novel structure of the complex with bound isoform-2 cytochrome c. Four core interactions encircle the heme cofactors surrounded by variable interactions. The core interface may be a feature to gain specificity for formation of the reactive complex.

Structure of complex III with bound cytochrome c in reduced state and definition of a minimal core interface for electron transfer.,Solmaz SR, Hunte C J Biol Chem. 2008 Jun 20;283(25):17542-9. Epub 2008 Apr 4. PMID:18390544^[1]

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

References

↑ Solmaz SR, Hunte C. Structure of complex III with bound cytochrome c in reduced state and definition of a minimal core interface for electron transfer. J Biol Chem. 2008 Jun 20;283(25):17542-9. Epub 2008 Apr 4. PMID:18390544 doi:10.1074/jbc.M710126200

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/3cx5"

@@ Line 1: / Line 1: @@
 ==Structure of complex III with bound cytochrome c in reduced state and definition of a minimal core interface for electron transfer.==
-<StructureSection load='3cx5' size='340' side='right' caption='[[3cx5]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
+<StructureSection load='3cx5' size='340' side='right'caption='[[3cx5]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[3cx5]] is a 23 chain structure with sequence from [http://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice] and [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3CX5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3CX5 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[3cx5]] is a 23 chain structure with sequence from [http://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice] and [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3CX5 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=3CX5 FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=6PH:(1R)-2-(PHOSPHONOOXY)-1-[(TRIDECANOYLOXY)METHYL]ETHYL+PENTADECANOATE'>6PH</scene>, <scene name='pdbligand=7PH:(1R)-2-(DODECANOYLOXY)-1-[(PHOSPHONOOXY)METHYL]ETHYL+TETRADECANOATE'>7PH</scene>, <scene name='pdbligand=8PE:(2R)-3-{[(S)-(2-AMINOETHOXY)(HYDROXY)PHOSPHORYL]OXY}-2-(TETRADECANOYLOXY)PROPYL+OCTADECANOATE'>8PE</scene>, <scene name='pdbligand=9PE:(1R)-2-{[(S)-(2-AMINOETHOXY)(HYDROXY)PHOSPHORYL]OXY}-1-[(HEPTANOYLOXY)METHYL]ETHYL+OCTADECANOATE'>9PE</scene>, <scene name='pdbligand=CN3:(2R,5S,11R,14R)-5,8,11-TRIHYDROXY-2-(NONANOYLOXY)-5,11-DIOXIDO-16-OXO-14-[(PROPANOYLOXY)METHYL]-4,6,10,12,15-PENTAOXA-5,11-DIPHOSPHANONADEC-1-YL+UNDECANOATE'>CN3</scene>, <scene name='pdbligand=CN5:(5S,11R)-5,8,11-TRIHYDROXY-5,11-DIOXIDO-17-OXO-4,6,10,12,16-PENTAOXA-5,11-DIPHOSPHAOCTADEC-1-YL+PENTADECANOATE'>CN5</scene>, <scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=SMA:STIGMATELLIN+A'>SMA</scene>, <scene name='pdbligand=SUC:SUCROSE'>SUC</scene>, <scene name='pdbligand=UMQ:UNDECYL-MALTOSIDE'>UMQ</scene></td></tr>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=6PH:(1R)-2-(PHOSPHONOOXY)-1-[(TRIDECANOYLOXY)METHYL]ETHYL+PENTADECANOATE'>6PH</scene>, <scene name='pdbligand=7PH:(1R)-2-(DODECANOYLOXY)-1-[(PHOSPHONOOXY)METHYL]ETHYL+TETRADECANOATE'>7PH</scene>, <scene name='pdbligand=8PE:(2R)-3-{[(S)-(2-AMINOETHOXY)(HYDROXY)PHOSPHORYL]OXY}-2-(TETRADECANOYLOXY)PROPYL+OCTADECANOATE'>8PE</scene>, <scene name='pdbligand=9PE:(1R)-2-{[(S)-(2-AMINOETHOXY)(HYDROXY)PHOSPHORYL]OXY}-1-[(HEPTANOYLOXY)METHYL]ETHYL+OCTADECANOATE'>9PE</scene>, <scene name='pdbligand=CN3:(2R,5S,11R,14R)-5,8,11-TRIHYDROXY-2-(NONANOYLOXY)-5,11-DIOXIDO-16-OXO-14-[(PROPANOYLOXY)METHYL]-4,6,10,12,15-PENTAOXA-5,11-DIPHOSPHANONADEC-1-YL+UNDECANOATE'>CN3</scene>, <scene name='pdbligand=CN5:(5S,11R)-5,8,11-TRIHYDROXY-5,11-DIOXIDO-17-OXO-4,6,10,12,16-PENTAOXA-5,11-DIPHOSPHAOCTADEC-1-YL+PENTADECANOATE'>CN5</scene>, <scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</scene>, <scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=SMA:STIGMATELLIN+A'>SMA</scene>, <scene name='pdbligand=UMQ:UNDECYL-MALTOSIDE'>UMQ</scene>, <scene name='pdbligand=FRU:FRUCTOSE'>FRU</scene></td></tr>
 <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=M3L:N-TRIMETHYLLYSINE'>M3L</scene></td></tr>
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3cxh|3cxh]], [[1ezv|1ezv]], [[1kb9|1kb9]], [[1kyo|1kyo]]</td></tr>
 <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Ubiquinol--cytochrome-c_reductase Ubiquinol--cytochrome-c reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.10.2.2 1.10.2.2] </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=3cx5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3cx5 OCA], [http://pdbe.org/3cx5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3cx5 RCSB], [http://www.ebi.ac.uk/pdbsum/3cx5 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3cx5 ProSAT]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=3cx5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3cx5 OCA], [http://pdbe.org/3cx5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3cx5 RCSB], [http://www.ebi.ac.uk/pdbsum/3cx5 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3cx5 ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 33: / Line 33: @@
 ==See Also==
+*[[Cytochrome C 3D structures|Cytochrome C 3D structures]]
 *[[Cytochrome bc1 complex|Cytochrome bc1 complex]]
-*[[Cytochrome c|Cytochrome c]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
+[[Category: Large Structures]]
 [[Category: Lk3 transgenic mice]]
 [[Category: Saccharomyces cerevisiae]]

3cx5

From Proteopedia

Revision as of 10:30, 12 August 2020

Structure of complex III with bound cytochrome c in reduced state and definition of a minimal core interface for electron transfer.

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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