6xkt: Difference between revisions
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==== | ==R. capsulatus cyt bc1 with both FeS proteins in c position (CIII2 c-c)== | ||
<StructureSection load='6xkt' size='340' side='right'caption='[[6xkt]]' scene=''> | <StructureSection load='6xkt' size='340' side='right'caption='[[6xkt]], [[Resolution|resolution]] 3.75Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id= OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol= FirstGlance]. <br> | <table><tr><td colspan='2'>[[6xkt]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Rhodobacter_capsulatus_SB_1003 Rhodobacter capsulatus SB 1003]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6XKT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6XKT FirstGlance]. <br> | ||
</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=6xkt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6xkt OCA], [https://pdbe.org/6xkt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6xkt RCSB], [https://www.ebi.ac.uk/pdbsum/6xkt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6xkt ProSAT]</span></td></tr> | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.75Å</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></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=6xkt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6xkt OCA], [https://pdbe.org/6xkt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6xkt RCSB], [https://www.ebi.ac.uk/pdbsum/6xkt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6xkt ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/CYB_RHOCB CYB_RHOCB] 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. | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Respiratory electron transport complexes are organized as individual entities or combined as large supercomplexes (SC). Gram-negative bacteria deploy a mitochondrial-like cytochrome (cyt) bc(1) (Complex III, CIII(2)), and may have specific cbb(3)-type cyt c oxidases (Complex IV, CIV) instead of the canonical aa(3)-type CIV. Electron transfer between these complexes is mediated by soluble (c(2)) and membrane-anchored (c(y)) cyts. Here, we report the structure of an engineered bc(1)-cbb(3) type SC (CIII(2)CIV, 5.2 A resolution) and three conformers of native CIII(2) (3.3 A resolution). The SC is active in vivo and in vitro, contains all catalytic subunits and cofactors, and two extra transmembrane helices attributed to cyt c(y) and the assembly factor CcoH. The cyt c(y) is integral to SC, its cyt domain is mobile and it conveys electrons to CIV differently than cyt c(2). The successful production of a native-like functional SC and determination of its structure illustrate the characteristics of membrane-confined and membrane-external respiratory electron transport pathways in Gram-negative bacteria. | |||
Cryo-EM structures of engineered active bc(1)-cbb(3) type CIII(2)CIV super-complexes and electronic communication between the complexes.,Steimle S, van Eeuwen T, Ozturk Y, Kim HJ, Braitbard M, Selamoglu N, Garcia BA, Schneidman-Duhovny D, Murakami K, Daldal F Nat Commun. 2021 Feb 10;12(1):929. doi: 10.1038/s41467-021-21051-4. PMID:33568648<ref>PMID:33568648</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 6xkt" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Cytochrome C 3D structures|Cytochrome C 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: | [[Category: Rhodobacter capsulatus SB 1003]] | ||
[[Category: Braitbard M]] | |||
[[Category: Daldal F]] | |||
[[Category: Garcia BA]] | |||
[[Category: Kim HJ]] | |||
[[Category: Murakami K]] | |||
[[Category: Ozturk Y]] | |||
[[Category: Schneidman-Duhovny D]] | |||
[[Category: Selamoglu N]] | |||
[[Category: Steimle S]] | |||
[[Category: Van Eeuwen T]] | |||