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8dbp
From Proteopedia
(Difference between revisions)
(New page: '''Unreleased structure''' The entry 8dbp is ON HOLD Authors: Sobti, M., Stewart, A.G. Description: E. coli ATP synthase imaged in 10mM MgATP State1 ""half-up [[Category: Unreleased St...) |
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| - | '''Unreleased structure''' | ||
| - | + | ==E. coli ATP synthase imaged in 10mM MgATP State1 "half-up== | |
| + | <StructureSection load='8dbp' size='340' side='right'caption='[[8dbp]], [[Resolution|resolution]] 3.60Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[8dbp]] is a 22 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8DBP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8DBP FirstGlance]. <br> | ||
| + | </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=8dbp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8dbp OCA], [https://pdbe.org/8dbp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8dbp RCSB], [https://www.ebi.ac.uk/pdbsum/8dbp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8dbp ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/F4TL55_ECOLX F4TL55_ECOLX] F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. 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.[HAMAP-Rule:MF_01396] Key component of the F(0) channel; it plays a direct role in translocation across the membrane. A homomeric c-ring of between 10-14 subunits forms the central stalk rotor element with the F(1) delta and epsilon subunits.[HAMAP-Rule:MF_01396] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | F(1)F(o) ATP synthase functions as a biological generator and makes a major contribution to cellular energy production. Proton flow generates rotation in the F(o) motor that is transferred to the F(1) motor to catalyze ATP production, with flexible F(1)/F(o) coupling required for efficient catalysis. F(1)F(o) ATP synthase can also operate in reverse, hydrolyzing ATP and pumping protons, and in bacteria this function can be regulated by an inhibitory epsilon subunit. Here we present cryo-EM data showing E. coli F(1)F(o) ATP synthase in different rotational and inhibited sub-states, observed following incubation with 10 mM MgATP. Our structures demonstrate how structural transitions within the inhibitory epsilon subunit induce torsional movement in the central stalk, thereby enabling its rotation within the F(omicron) motor. This highlights the importance of the central rotor for flexible coupling of the F(1) and F(o) motors and provides further insight into the regulatory mechanism mediated by subunit epsilon. | ||
| - | + | Changes within the central stalk of E. coli F(1)F(o) ATP synthase observed after addition of ATP.,Sobti M, Zeng YC, Walshe JL, Brown SHJ, Ishmukhametov R, Stewart AG Commun Biol. 2023 Jan 11;6(1):26. doi: 10.1038/s42003-023-04414-z. PMID:36631659<ref>PMID:36631659</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| - | [[Category: Sobti | + | <div class="pdbe-citations 8dbp" style="background-color:#fffaf0;"></div> |
| - | [[Category: Stewart | + | == References == |
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Escherichia coli]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Sobti M]] | ||
| + | [[Category: Stewart AG]] | ||
Current revision
E. coli ATP synthase imaged in 10mM MgATP State1 "half-up
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