6j5j: Difference between revisions
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New page: '''Unreleased structure''' The entry 6j5j is ON HOLD Authors: Zhang, L.X., Yi, J.B. Description: 3 Category: Unreleased Structures Category: Zhang, L.X Category: Yi, J.B |
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==Cryo-EM structure of the mammalian E-state ATP synthase== | |||
<SX load='6j5j' size='340' side='right' viewer='molstar' caption='[[6j5j]], [[Resolution|resolution]] 3.45Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6j5j]] is a 14 chain structure with sequence from [https://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6J5J OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6J5J 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]] 3.45Å</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=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=6j5j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6j5j OCA], [https://pdbe.org/6j5j PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6j5j RCSB], [https://www.ebi.ac.uk/pdbsum/6j5j PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6j5j ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/ATPA_PIG ATPA_PIG] 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. Subunits alpha and beta form the catalytic core in F(1). Rotation of the central stalk against the surrounding alpha(3)beta(3) subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits. Subunit alpha does not bear the catalytic high-affinity ATP-binding sites (By similarity). Binds the bacterial siderophore enterobactin and can promote mitochondrial accumulation of enterobactin-derived iron ions (By similarity).[UniProtKB:P19483][UniProtKB:P25705] | |||
==See Also== | |||
*[[ATPase 3D structures|ATPase 3D structures]] | |||
__TOC__ | |||
[[Category: | </SX> | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: Yi | [[Category: Sus scrofa]] | ||
[[Category: Gu J]] | |||
[[Category: Yang M]] | |||
[[Category: Yi J]] | |||
[[Category: Zhang L]] | |||
Latest revision as of 10:36, 27 March 2024
Cryo-EM structure of the mammalian E-state ATP synthase
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