6wnq
From Proteopedia
(Difference between revisions)
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- | == | + | ==n/a== |
- | <StructureSection load='6wnq' size='340' side='right'caption='[[6wnq]] | + | <StructureSection load='6wnq' size='340' side='right'caption='[[6wnq]]' scene=''> |
== Structural highlights == | == Structural highlights == | ||
- | <table><tr><td colspan='2'> | + | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6WNQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6WNQ FirstGlance]. <br> |
- | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy</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=6wnq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6wnq OCA], [https://pdbe.org/6wnq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6wnq RCSB], [https://www.ebi.ac.uk/pdbsum/6wnq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6wnq ProSAT]</span></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=6wnq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6wnq OCA], [https://pdbe.org/6wnq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6wnq RCSB], [https://www.ebi.ac.uk/pdbsum/6wnq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6wnq ProSAT]</span></td></tr> | ||
</table> | </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] | ||
==See Also== | ==See Also== | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
- | [[Category: Escherichia coli]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
- | [[Category: | + | [[Category: N/a]] |
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Current revision
n/a
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