8ap7: Difference between revisions
New page: '''Unreleased structure''' The entry 8ap7 is ON HOLD Authors: Description: Category: Unreleased Structures |
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The | ==membrane region of the Trypanosoma brucei mitochondrial ATP synthase dimer== | ||
<StructureSection load='8ap7' size='340' side='right'caption='[[8ap7]], [[Resolution|resolution]] 2.70Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[8ap7]] is a 20 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=8AP7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8AP7 FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AME:N-ACETYLMETHIONINE'>AME</scene>, <scene name='pdbligand=CDL:CARDIOLIPIN'>CDL</scene>, <scene name='pdbligand=LMT:DODECYL-BETA-D-MALTOSIDE'>LMT</scene>, <scene name='pdbligand=PC1:1,2-DIACYL-SN-GLYCERO-3-PHOSPHOCHOLINE'>PC1</scene>, <scene name='pdbligand=PEE:1,2-DIOLEOYL-SN-GLYCERO-3-PHOSPHOETHANOLAMINE'>PEE</scene>, <scene name='pdbligand=Q7G:2-{[(4-O-alpha-D-glucopyranosyl-alpha-D-glucopyranosyl)oxy]methyl}-4-{[(3beta,9beta,14beta,17beta,25R)-spirost-5-en-3-yl]oxy}butyl+4-O-alpha-D-glucopyranosyl-alpha-D-glucopyranoside'>Q7G</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=8ap7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8ap7 OCA], [https://pdbe.org/8ap7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8ap7 RCSB], [https://www.ebi.ac.uk/pdbsum/8ap7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8ap7 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/Q57VT0_TRYB2 Q57VT0_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. | |||
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> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 8ap7" 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]] | |||
Latest revision as of 09:09, 26 October 2022
membrane region of the Trypanosoma brucei mitochondrial ATP synthase dimermembrane region of the Trypanosoma brucei mitochondrial ATP synthase dimer
Structural highlights
FunctionPublication Abstract from PubMedMitochondrial 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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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