8dbu: Difference between revisions
No edit summary |
No edit summary |
||
Line 1: | Line 1: | ||
The | ==E. coli ATP synthase imaged in 10mM MgATP State2 "down" Fo classified== | ||
<StructureSection load='8dbu' size='340' side='right'caption='[[8dbu]], [[Resolution|resolution]] 3.40Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[8dbu]] 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=8DBU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8DBU 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=8dbu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8dbu OCA], [https://pdbe.org/8dbu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8dbu RCSB], [https://www.ebi.ac.uk/pdbsum/8dbu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8dbu ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/A0A7U9G3U3_ECOLX A0A7U9G3U3_ECOLX] Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit.[ARBA:ARBA00003784][HAMAP-Rule:MF_01346] | |||
<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 8dbu" style="background-color:#fffaf0;"></div> | ||
[[Category: Stewart | == References == | ||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Escherichia coli]] | |||
[[Category: Large Structures]] | |||
[[Category: Sobti M]] | |||
[[Category: Stewart AG]] |
Revision as of 09:36, 25 January 2023
E. coli ATP synthase imaged in 10mM MgATP State2 "down" Fo classifiedE. coli ATP synthase imaged in 10mM MgATP State2 "down" Fo classified
Structural highlights
FunctionA0A7U9G3U3_ECOLX Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit.[ARBA:ARBA00003784][HAMAP-Rule:MF_01346] Publication Abstract from PubMedF(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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
|
|