9w2r: Difference between revisions
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==Cryo-EM structure of FoF1-ATPase monomer state 1 on the bovine heart submitochondrial particles (FoF1-1)== | |||
<StructureSection load='9w2r' size='340' side='right'caption='[[9w2r]], [[Resolution|resolution]] 3.40Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[9w2r]] is a 21 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9W2R OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9W2R 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]] 3.4Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=M3L:N-TRIMETHYLLYSINE'>M3L</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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=9w2r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9w2r OCA], [https://pdbe.org/9w2r PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9w2r RCSB], [https://www.ebi.ac.uk/pdbsum/9w2r PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9w2r ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/ATP8_BOVIN ATP8_BOVIN] Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(0) domain. Minor subunit located with subunit a in the membrane (By similarity). | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Understanding the functional mechanisms of membrane protein complexes requires structural analysis within their native membrane environment. Here, we applied cryo-electron microscopy to determine the structures of F(o)F(1) ATP synthase and respiratory supercomplexes (SCs) on sub-mitochondrial particles (SMPs) isolated from bovine heart mitochondria. Most F(o)F(1) complexes were observed as dimers stabilized by the regulatory factor IF(1), and a tetrameric assembly comprising two F(o)F(1)-IF(1) dimers arranged linearly was also identified. This finding indicates that the tetrameric units of F(o)F(1) are present in the mitochondrial inner membrane and contribute to shaping cristae tips in mammalian mitochondria. F(o) domain maps resolve the e-subunit- c(8)-ring interface and show no discrete density for a tightly bound lipid within the c(8)-ring. In addition to the previously reported SCs compositions CI(1)CIII(2)CIV(1) and CI(1)CIII(2)CIV(2), our analysis identified an additional assembly with the composition CI(1)CIII(2)CIV(3), as well as a CI(2)CIII(2)CIV(6) mega-complex. This approach enables rapid structural determination of F(o)F(1) ATP synthase and SCs from minimal membrane fractions, providing a foundation for elucidating the molecular basis of metabolic disorders and mitochondrial diseases at the level of higher-order architecture. | |||
Structures of respiratory supercomplexes and ATP synthase oligomers in mammalian mitochondrial inner membrane.,Nakano A, Masuya T, Akisada S, Ishikawa-Fukuda M, Mitsuoka K, Miyoshi H, Murai M, Yokoyama K Nat Commun. 2026 Mar 17. doi: 10.1038/s41467-026-70578-x. PMID:41844608<ref>PMID:41844608</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: Akisada | <div class="pdbe-citations 9w2r" style="background-color:#fffaf0;"></div> | ||
[[Category: | == References == | ||
[[Category: | <references/> | ||
[[Category: | __TOC__ | ||
[[Category: Miyoshi | </StructureSection> | ||
[[Category: Murai | [[Category: Bos taurus]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Akisada S]] | ||
[[Category: Ishikawa-Fukuda M]] | |||
[[Category: Masuya T]] | |||
[[Category: Mitsuoka K]] | |||
[[Category: Miyoshi H]] | |||
[[Category: Murai M]] | |||
[[Category: Nakano A]] | |||
[[Category: Yokoyama K]] | |||
Latest revision as of 16:03, 1 April 2026
Cryo-EM structure of FoF1-ATPase monomer state 1 on the bovine heart submitochondrial particles (FoF1-1)
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