8ap8: Difference between revisions

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'''Unreleased structure'''


The entry 8ap8 is ON HOLD  until Paper Publication
==Peripheral stalk of Trypanosoma brucei mitochondrial ATP synthase==
<StructureSection load='8ap8' size='340' side='right'caption='[[8ap8]], [[Resolution|resolution]] 3.70&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[8ap8]] is a 5 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=8AP8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8AP8 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=8ap8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8ap8 OCA], [https://pdbe.org/8ap8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8ap8 RCSB], [https://www.ebi.ac.uk/pdbsum/8ap8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8ap8 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q38AG1_TRYB2 Q38AG1_TRYB2]
<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 8ap8" 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]]
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