8ap9: Difference between revisions

From Proteopedia
Jump to navigationJump to search
OCA (talk | contribs)
m Protected "8ap9" [edit=sysop:move=sysop]
OCA (talk | contribs)
No edit summary
Line 1: Line 1:
'''Unreleased structure'''


The entry 8ap9 is ON HOLD
==rotor of the Trypanosoma brucei mitochondrial ATP synthase dimer==
<StructureSection load='8ap9' size='340' side='right'caption='[[8ap9]], [[Resolution|resolution]] 3.70&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[8ap9]] is a 13 chain structure with sequence from [https://en.wikipedia.org/wiki/Trypanosoma_brucei_brucei Trypanosoma brucei brucei]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8AP9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8AP9 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=UTP:URIDINE+5-TRIPHOSPHATE'>UTP</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=8ap9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8ap9 OCA], [https://pdbe.org/8ap9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8ap9 RCSB], [https://www.ebi.ac.uk/pdbsum/8ap9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8ap9 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A0A161CM65_TRYBB A0A161CM65_TRYBB]
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Mitochondrial ATP synthase forms stable dimers arranged into oligomeric assemblies that generate the inner-membrane curvature essential for efficient energy conversion. Here, we report cryo-EM structures of the intact ATP synthase dimer from Trypanosoma brucei in ten different rotational states. The model consists of 25 subunits, including nine lineage-specific, as well as 36 lipids. The rotary mechanism is influenced by the divergent peripheral stalk, conferring a greater conformational flexibility. Proton transfer in the lumenal half-channel occurs via a chain of five ordered water molecules. The dimerization interface is formed by subunit-g that is critical for interactions but not for the catalytic activity. Although overall dimer architecture varies among eukaryotes, we find that subunit-g together with subunit-e form an ancestral oligomerization motif, which is shared between the trypanosomal and mammalian lineages. Therefore, our data defines the subunit-g/e module as a structural component determining ATP synthase oligomeric assemblies.


Authors:  
An ancestral interaction module promotes oligomerization in divergent mitochondrial ATP synthases.,Gahura O, Muhleip A, Hierro-Yap C, Panicucci B, Jain M, Hollaus D, Slapnickova M, Zikova A, Amunts A Nat Commun. 2022 Oct 11;13(1):5989. doi: 10.1038/s41467-022-33588-z. PMID:36220811<ref>PMID:36220811</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 8ap9" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Trypanosoma brucei brucei]]
[[Category: Amunts A]]
[[Category: Gahura O]]
[[Category: Muehleip A]]
[[Category: Zikova A]]