9o1e: Difference between revisions

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'''Unreleased structure'''


The entry 9o1e is ON HOLD  until Paper Publication
==Pseudomonas aeruginosa ATPase State2a Fo focused==
 
<StructureSection load='9o1e' size='340' side='right'caption='[[9o1e]], [[Resolution|resolution]] 2.59&Aring;' scene=''>
Authors: Stewart, A.G., Sobti, M.
== Structural highlights ==
 
<table><tr><td colspan='2'>[[9o1e]] is a 13 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_aeruginosa Pseudomonas aeruginosa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9O1E OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9O1E FirstGlance]. <br>
Description: Pseudomonas aeruginosa ATPase State2a Fo focused
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 2.59&#8491;</td></tr>
[[Category: Unreleased Structures]]
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
[[Category: Stewart, A.G]]
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=9o1e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9o1e OCA], [https://pdbe.org/9o1e PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9o1e RCSB], [https://www.ebi.ac.uk/pdbsum/9o1e PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9o1e ProSAT]</span></td></tr>
[[Category: Sobti, M]]
</table>
== Function ==
[https://www.uniprot.org/uniprot/ATPL_PSEP7 ATPL_PSEP7] 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.  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.
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Pseudomonas aeruginosa]]
[[Category: Sobti M]]
[[Category: Stewart AG]]