6rwt: Difference between revisions
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==Crystal structure of the Cbp3 homolog from Brucella abortus== | |||
<StructureSection load='6rwt' size='340' side='right'caption='[[6rwt]], [[Resolution|resolution]] 1.42Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6rwt]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Brucella_abortus_nctc_8038 Brucella abortus nctc 8038]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6RWT OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6RWT FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> | |||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">BAUG_1320 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=575591 Brucella abortus NCTC 8038])</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=6rwt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6rwt OCA], [http://pdbe.org/6rwt PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6rwt RCSB], [http://www.ebi.ac.uk/pdbsum/6rwt PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6rwt ProSAT]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Assembly of the mitochondrial respiratory chain requires the coordinated synthesis of mitochondrial and nuclear encoded subunits, redox co-factor acquisition, and correct joining of the subunits to form functional complexes. The conserved Cbp3-Cbp6 chaperone complex binds newly synthesized cytochrome b and supports the ordered acquisition of the heme co-factors. Moreover, it functions as a translational activator by interacting with the mitoribosome. Cbp3 consists of two distinct domains: an N-terminal domain present in mitochondrial Cbp3 homologs and a highly conserved C-terminal domain comprising a ubiquinol-cytochrome c chaperone region. Here, we solved the crystal structure of this C-terminal domain from a bacterial homolog at 1.4 A resolution, revealing a unique all-helical fold. This structure allowed mapping of the interaction sites of yeast Cbp3 with Cbp6 and cytochrome b via site-specific photo-cross-linking. We propose that mitochondrial Cbp3 homologs carry an N-terminal extension that positions the conserved C-terminal domain at the ribosomal tunnel exit for an efficient interaction with its substrate, the newly synthesized cytochrome b protein. | |||
Structural basis for the interaction of the chaperone Cbp3 with newly synthesized cytochrome b during mitochondrial respiratory chain assembly.,Ndi M, Masuyer G, Dawitz H, Carlstrom A, Michel M, Elofsson A, Rapp M, Stenmark P, Ott M J Biol Chem. 2019 Nov 8;294(45):16663-16671. doi: 10.1074/jbc.RA119.010483. Epub , 2019 Sep 19. PMID:31537648<ref>PMID:31537648</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 6rwt" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Brucella abortus nctc 8038]] | |||
[[Category: Large Structures]] | |||
[[Category: Masuyer, G]] | |||
[[Category: Ndi, M]] | |||
[[Category: Ott, M]] | |||
[[Category: Stenmark, P]] | |||
[[Category: Assembly factor]] | |||
[[Category: Chaperone]] | |||
[[Category: Complex iii]] | |||
[[Category: Mitochondrial translation]] | |||
[[Category: Respiratory chain]] | |||
