1be3
From Proteopedia
(Difference between revisions)
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<StructureSection load='1be3' size='340' side='right'caption='[[1be3]], [[Resolution|resolution]] 3.00Å' scene=''> | <StructureSection load='1be3' size='340' side='right'caption='[[1be3]], [[Resolution|resolution]] 3.00Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
- | <table><tr><td colspan='2'>[[1be3]] is a | + | <table><tr><td colspan='2'>[[1be3]] is a 10 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BE3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1BE3 FirstGlance]. <br> |
- | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</scene>, <scene name='pdbligand=HEC:HEME+C'>HEC</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3Å</td></tr> |
- | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</scene>, <scene name='pdbligand=HEC:HEME+C'>HEC</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</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=1be3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1be3 OCA], [https://pdbe.org/1be3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1be3 RCSB], [https://www.ebi.ac.uk/pdbsum/1be3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1be3 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=1be3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1be3 OCA], [https://pdbe.org/1be3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1be3 RCSB], [https://www.ebi.ac.uk/pdbsum/1be3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1be3 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
- | + | [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 == | == 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=1be3 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=1be3 ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
- | <div style="background-color:#fffaf0;"> | ||
- | == Publication Abstract from PubMed == | ||
- | Mitochondrial cytochrome bc1 complex performs two functions: It is a respiratory multienzyme complex and it recognizes a mitochondrial targeting presequence. Refined crystal structures of the 11-subunit bc1 complex from bovine heart reveal full views of this bifunctional enzyme. The "Rieske" iron-sulfur protein subunit shows significant conformational changes in different crystal forms, suggesting a new electron transport mechanism of the enzyme. The mitochondrial targeting presequence of the "Rieske" protein (subunit 9) is lodged between the two "core" subunits at the matrix side of the complex. These "core" subunits are related to the matrix processing peptidase, and the structure unveils how mitochondrial targeting presequences are recognized. | ||
- | |||
- | Complete structure of the 11-subunit bovine mitochondrial cytochrome bc1 complex.,Iwata S, Lee JW, Okada K, Lee JK, Iwata M, Rasmussen B, Link TA, Ramaswamy S, Jap BK Science. 1998 Jul 3;281(5373):64-71. PMID:9651245<ref>PMID:9651245</ref> | ||
- | |||
- | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
- | </div> | ||
- | <div class="pdbe-citations 1be3" 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]] | ||
- | *[[Cytochrome bc1 | + | *[[Cytochrome bc1 3D structures|Cytochrome bc1 3D structures]] |
- | + | ||
- | + | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Bos taurus]] | [[Category: Bos taurus]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
- | + | [[Category: Iwata M]] | |
- | [[Category: Iwata | + | [[Category: Iwata S]] |
- | [[Category: Iwata | + | [[Category: Jap BK]] |
- | [[Category: Jap | + | [[Category: Lee JK]] |
- | [[Category: Lee | + | [[Category: Lee JW]] |
- | [[Category: Lee | + | [[Category: Okada K]] |
- | [[Category: Okada | + | [[Category: Ramaswamy S]] |
- | [[Category: Ramaswamy | + | |
- | + | ||
- | + | ||
- | + |
Revision as of 15:32, 13 March 2024
CYTOCHROME BC1 COMPLEX FROM BOVINE
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Categories: Bos taurus | Large Structures | Iwata M | Iwata S | Jap BK | Lee JK | Lee JW | Okada K | Ramaswamy S