7ssp: Difference between revisions

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New page: '''Unreleased structure''' The entry 7ssp is ON HOLD Authors: Description: Category: Unreleased Structures
 
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'''Unreleased structure'''


The entry 7ssp is ON HOLD
==Structure of the human COQ7:COQ9 complex by single-particle electron cryo-microscopy, unliganded state==
<StructureSection load='7ssp' size='340' side='right'caption='[[7ssp]], [[Resolution|resolution]] 3.50&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[7ssp]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7SSP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7SSP 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]] 3.5&#8491;</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=7ssp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7ssp OCA], [https://pdbe.org/7ssp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7ssp RCSB], [https://www.ebi.ac.uk/pdbsum/7ssp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7ssp ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/COQ9_HUMAN COQ9_HUMAN]
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Coenzyme Q (CoQ) is a redox-active lipid essential for core metabolic pathways and antioxidant defense. CoQ is synthesized upon the mitochondrial inner membrane by an ill-defined "complex Q" metabolon. Here, we present structure-function analyses of a lipid-, substrate-, and NADH-bound complex comprising two complex Q subunits: the hydroxylase COQ7 and the lipid-binding protein COQ9. We reveal that COQ7 adopts a ferritin-like fold with a hydrophobic channel whose substrate-binding capacity is enhanced by COQ9. Using molecular dynamics, we further show that two COQ7:COQ9 heterodimers form a curved tetramer that deforms the membrane, potentially opening a pathway for the CoQ intermediates to translocate from the bilayer to the proteins' lipid-binding sites. Two such tetramers assemble into a soluble octamer with a pseudo-bilayer of lipids captured within. Together, these observations indicate that COQ7 and COQ9 cooperate to access hydrophobic precursors within the membrane and coordinate subsequent synthesis steps toward producing CoQ.


Authors:  
Structure and functionality of a multimeric human COQ7:COQ9 complex.,Manicki M, Aydin H, Abriata LA, Overmyer KA, Guerra RM, Coon JJ, Dal Peraro M, Frost A, Pagliarini DJ Mol Cell. 2022 Nov 17;82(22):4307-4323.e10. doi: 10.1016/j.molcel.2022.10.003. , Epub 2022 Oct 27. PMID:36306796<ref>PMID:36306796</ref>


Description:  
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Unreleased Structures]]
</div>
<div class="pdbe-citations 7ssp" style="background-color:#fffaf0;"></div>
 
==See Also==
*[[Elongation factor 3D structures|Elongation factor 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Aydin H]]
[[Category: Frost A]]

Latest revision as of 05:52, 5 June 2024

Structure of the human COQ7:COQ9 complex by single-particle electron cryo-microscopy, unliganded state

7ssp, resolution 3.50Å

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