6xku: Difference between revisions
No edit summary |
No edit summary |
||
| (2 intermediate revisions by the same user not shown) | |||
| Line 1: | Line 1: | ||
==R. capsulatus cyt bc1 with one FeS protein in b position and one in c position (CIII2 b-c)== | |||
<StructureSection load='6xku' size='340' side='right'caption='[[6xku]], [[Resolution|resolution]] 4.20Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6xku]] 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=6XKU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6XKU FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 4.2Å</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=6xku FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6xku OCA], [https://pdbe.org/6xku PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6xku RCSB], [https://www.ebi.ac.uk/pdbsum/6xku PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6xku ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/UCRI_RHOCB UCRI_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> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 6xku" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Cytochrome C 3D structures|Cytochrome C 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[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]] | |||
Latest revision as of 08:57, 21 November 2024
R. capsulatus cyt bc1 with one FeS protein in b position and one in c position (CIII2 b-c)R. capsulatus cyt bc1 with one FeS protein in b position and one in c position (CIII2 b-c)
Structural highlights
FunctionUCRI_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. Publication Abstract from PubMedRespiratory 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
|
| ||||||||||||||||||