6ynv: Difference between revisions
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The | ==Cryo-EM structure of Tetrahymena thermophila mitochondrial ATP synthase - Fo-wing region== | ||
<StructureSection load='6ynv' size='340' side='right'caption='[[6ynv]], [[Resolution|resolution]] 2.80Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6ynv]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Tetrahymena_thermophila Tetrahymena thermophila]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6YNV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6YNV 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]] 2.8Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</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=6ynv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ynv OCA], [https://pdbe.org/6ynv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6ynv RCSB], [https://www.ebi.ac.uk/pdbsum/6ynv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6ynv ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/I7LVQ8_TETTS I7LVQ8_TETTS] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Mitochondrial ATP synthases form functional homodimers to induce cristae curvature that is a universal property of mitochondria. To expand on the understanding of this fundamental phenomenon, we characterized the unique type III mitochondrial ATP synthase in its dimeric and tetrameric form. The cryo-EM structure of a ciliate ATP synthase dimer reveals an unusual U-shaped assembly of 81 proteins, including a substoichiometrically bound ATPTT2, 40 lipids, and co-factors NAD and CoQ. A single copy of subunit ATPTT2 functions as a membrane anchor for the dimeric inhibitor IF1. Type III specific linker proteins stably tie the ATP synthase monomers in parallel to each other. The intricate dimer architecture is scaffolded by an extended subunit-a that provides a template for both intra- and inter-dimer interactions. The latter results in the formation of tetramer assemblies, the membrane part of which we determined to 3.1 A resolution. The structure of the type III ATP synthase tetramer and its associated lipids suggests that it is the intact unit propagating the membrane curvature. | |||
Type III ATP synthase is a symmetry-deviated dimer that induces membrane curvature through tetramerization.,Flygaard RK, Muhleip A, Tobiasson V, Amunts A Nat Commun. 2020 Oct 22;11(1):5342. doi: 10.1038/s41467-020-18993-6. PMID:33093501<ref>PMID:33093501</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 6ynv" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[ATPase 3D structures|ATPase 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Tetrahymena thermophila]] | |||
[[Category: Amunts A]] | |||
[[Category: Kock Flygaard R]] | |||
[[Category: Muhleip A]] | |||
Latest revision as of 13:21, 22 May 2024
Cryo-EM structure of Tetrahymena thermophila mitochondrial ATP synthase - Fo-wing regionCryo-EM structure of Tetrahymena thermophila mitochondrial ATP synthase - Fo-wing region
Structural highlights
FunctionPublication Abstract from PubMedMitochondrial ATP synthases form functional homodimers to induce cristae curvature that is a universal property of mitochondria. To expand on the understanding of this fundamental phenomenon, we characterized the unique type III mitochondrial ATP synthase in its dimeric and tetrameric form. The cryo-EM structure of a ciliate ATP synthase dimer reveals an unusual U-shaped assembly of 81 proteins, including a substoichiometrically bound ATPTT2, 40 lipids, and co-factors NAD and CoQ. A single copy of subunit ATPTT2 functions as a membrane anchor for the dimeric inhibitor IF1. Type III specific linker proteins stably tie the ATP synthase monomers in parallel to each other. The intricate dimer architecture is scaffolded by an extended subunit-a that provides a template for both intra- and inter-dimer interactions. The latter results in the formation of tetramer assemblies, the membrane part of which we determined to 3.1 A resolution. The structure of the type III ATP synthase tetramer and its associated lipids suggests that it is the intact unit propagating the membrane curvature. Type III ATP synthase is a symmetry-deviated dimer that induces membrane curvature through tetramerization.,Flygaard RK, Muhleip A, Tobiasson V, Amunts A Nat Commun. 2020 Oct 22;11(1):5342. doi: 10.1038/s41467-020-18993-6. PMID:33093501[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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