1bcc

From Proteopedia

(Difference between revisions)

Current revision

CYTOCHROME BC1 COMPLEX FROM CHICKEN

Structural highlights

1bcc is a 10 chain structure with sequence from Gallus gallus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 3.16Å
Ligands:	, , , ,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

QCR1_BOVIN This is a component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex), which is part of the mitochondrial respiratory chain. This protein may mediate formation of the complex between cytochromes c and c1.

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

The cytochrome bc1 is one of the three major respiratory enzyme complexes residing in the inner mitochondrial membrane. Cytochrome bc1 transfers electrons from ubiquinol to cytochrome c and uses the energy thus released to form an electrochemical gradient across the inner membrane. Our X-ray crystal structures of the complex from chicken, cow and rabbit in both the presence and absence of inhibitors of quinone oxidation, reveal two different locations for the extrinsic domain of one component of the enzyme, an iron-sulphur protein. One location is close enough to the supposed quinol oxidation site to allow reduction of the Fe-S protein by ubiquinol. The other site is close enough to cytochrome c1 to allow oxidation of the Fe-S protein by the cytochrome. As neither location will allow both reactions to proceed at a suitable rate, the reaction mechanism must involve movement of the extrinsic domain of the Fe-S component in order to shuttle electrons from ubiquinol to cytochrome c1. Such a mechanism has not previously been observed in redox protein complexes.

Electron transfer by domain movement in cytochrome bc1.,Zhang Z, Huang L, Shulmeister VM, Chi YI, Kim KK, Hung LW, Crofts AR, Berry EA, Kim SH Nature. 1998 Apr 16;392(6677):677-84. PMID:9565029^[1]

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

References

↑ Zhang Z, Huang L, Shulmeister VM, Chi YI, Kim KK, Hung LW, Crofts AR, Berry EA, Kim SH. Electron transfer by domain movement in cytochrome bc1. Nature. 1998 Apr 16;392(6677):677-84. PMID:9565029 doi:10.1038/33612

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/1bcc"

@@ Line 3: / Line 3: @@
 <StructureSection load='1bcc' size='340' side='right'caption='[[1bcc]], [[Resolution|resolution]] 3.16&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1bcc]] is a 10 chain structure with sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BCC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1BCC FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1bcc]] is a 10 chain structure with sequence from [https://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BCC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1BCC FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BOG:B-OCTYLGLUCOSIDE'>BOG</scene>, <scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=PEE:1,2-DIOLEOYL-SN-GLYCERO-3-PHOSPHOETHANOLAMINE'>PEE</scene>, <scene name='pdbligand=U10:UBIQUINONE-10'>U10</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]] 3.16&#8491;</td></tr>
-<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=UNK:UNKNOWN'>UNK</scene></td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BOG:B-OCTYLGLUCOSIDE'>BOG</scene>, <scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=PEE:1,2-DIOLEOYL-SN-GLYCERO-3-PHOSPHOETHANOLAMINE'>PEE</scene>, <scene name='pdbligand=U10:UBIQUINONE-10'>U10</scene></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'>[https://proteopedia.org/fgij/fg.htm?mol=1bcc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bcc OCA], [https://pdbe.org/1bcc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1bcc RCSB], [https://www.ebi.ac.uk/pdbsum/1bcc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1bcc 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=1bcc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bcc OCA], [http://pdbe.org/1bcc PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1bcc RCSB], [http://www.ebi.ac.uk/pdbsum/1bcc PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1bcc ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/CYB_CHICK CYB_CHICK]] 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 (By similarity). [[http://www.uniprot.org/uniprot/QCR2_BOVIN QCR2_BOVIN]] This is a component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex), which is part of the mitochondrial respiratory chain. The core protein 2 is required for the assembly of the complex. [[http://www.uniprot.org/uniprot/QCR6_BOVIN QCR6_BOVIN]] This is a component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex), which is part of the mitochondrial respiratory chain. This protein may mediate formation of the complex between cytochromes c and c1. [[http://www.uniprot.org/uniprot/UCRI_BOVIN UCRI_BOVIN]] 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 transit peptide of the Rieske protein seems to form part of the bc1 complex and is considered to be the subunit 11/IX of that complex. [[http://www.uniprot.org/uniprot/CY1_BOVIN CY1_BOVIN]] This is the heme-containing component of the cytochrome b-c1 complex, which accepts electrons from Rieske protein and transfers electrons to cytochrome c in the mitochondrial respiratory chain. [[http://www.uniprot.org/uniprot/QCR9_BOVIN QCR9_BOVIN]] This is a component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex), which is part of the mitochondrial respiratory chain. This subunit interacts with cytochrome c1.
+[https://www.uniprot.org/uniprot/QCR1_BOVIN QCR1_BOVIN] This is a component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex), which is part of the mitochondrial respiratory chain. This protein may mediate formation of the complex between cytochromes c and c1.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 16: / Line 15: @@
   <jmolCheckbox>
     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/bc/1bcc_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>
@@ Line 33: / Line 32: @@
 ==See Also==
 *[[Cytochrome C 3D structures|Cytochrome C 3D structures]]
-*[[Cytochrome bc1 complex|Cytochrome bc1 complex]]
+*[[Cytochrome bc1 3D structures|Cytochrome bc1 3D structures]]
 == References ==
 <references/>
@@ Line 40: / Line 39: @@
 [[Category: Gallus gallus]]
 [[Category: Large Structures]]
-[[Category: Ubiquinol--cytochrome-c reductase]]
+[[Category: Berry EA]]
-[[Category: Berry, E A]]
+[[Category: Chi Y-I]]
-[[Category: Chi, Y I]]
+[[Category: Crofts AR]]
-[[Category: Crofts, A R]]
+[[Category: Huang L]]
-[[Category: Huang, L]]
+[[Category: Hung L-W]]
-[[Category: Hung, L W]]
+[[Category: Kim KK]]
-[[Category: Kim, K K]]
+[[Category: Kim S-H]]
-[[Category: Kim, S H]]
+[[Category: Shulmeister VM]]
-[[Category: Shulmeister, V M]]
+[[Category: Zhang Z]]
-[[Category: Zhang, Z]]
-[[Category: Electron transport]]
-[[Category: Membrane protein]]
-[[Category: Oxidoreductase]]
-[[Category: Redox enzyme]]
-[[Category: Respiratory chain]]
-[[Category: Ubiquinone]]

1bcc

From Proteopedia

Current revision

CYTOCHROME BC1 COMPLEX FROM CHICKEN

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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