6oqv: Difference between revisions

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'''Unreleased structure'''


The entry 6oqv is ON HOLD
==E. coli ATP Synthase State 2b==
<StructureSection load='6oqv' size='340' side='right'caption='[[6oqv]], [[Resolution|resolution]] 3.30&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6oqv]] 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=6OQV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6OQV 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]] 3.3&#8491;</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>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</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=6oqv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6oqv OCA], [https://pdbe.org/6oqv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6oqv RCSB], [https://www.ebi.ac.uk/pdbsum/6oqv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6oqv ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/ATPD_ECOLI ATPD_ECOLI] 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_01416]  This protein is part of the stalk that links CF(0) to CF(1). It either transmits conformational changes from CF(0) to CF(1) or is implicated in proton conduction.[HAMAP-Rule:MF_01416]


Authors:  
==See Also==
 
*[[ATPase 3D structures|ATPase 3D structures]]
Description:  
__TOC__
[[Category: Unreleased Structures]]
</StructureSection>
[[Category: Escherichia coli]]
[[Category: Large Structures]]
[[Category: Sobti M]]
[[Category: Stewart AG]]
[[Category: Walshe JL]]