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2wgm
From Proteopedia
(Difference between revisions)
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2wgm]] is a 44 chain structure with sequence from [http://en.wikipedia.org/wiki/Ilyobacter_tartaricus Ilyobacter tartaricus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2WGM OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2WGM FirstGlance]. <br> | <table><tr><td colspan='2'>[[2wgm]] is a 44 chain structure with sequence from [http://en.wikipedia.org/wiki/Ilyobacter_tartaricus Ilyobacter tartaricus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2WGM OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2WGM FirstGlance]. <br> | ||
| - | </td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=F09:NONAN-1-OL'>F09</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>< | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=F09:NONAN-1-OL'>F09</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr> |
| - | <tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1yce|1yce]]</td></tr> | + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1yce|1yce]]</td></tr> |
| - | <tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2wgm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2wgm OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2wgm RCSB], [http://www.ebi.ac.uk/pdbsum/2wgm PDBsum]</span></td></tr> | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2wgm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2wgm OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2wgm RCSB], [http://www.ebi.ac.uk/pdbsum/2wgm PDBsum]</span></td></tr> |
| - | <table> | + | </table> |
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/ATPL_ILYTA ATPL_ILYTA]] 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 sodium 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 sodium 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 11 subunits forms the central stalk rotor element with the F(1) delta and epsilon subunits.[HAMAP-Rule:MF_01396] | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Ilyobacter tartaricus]] | [[Category: Ilyobacter tartaricus]] | ||
| - | [[Category: Diederichs, K | + | [[Category: Diederichs, K]] |
| - | [[Category: Meier, T | + | [[Category: Meier, T]] |
| - | [[Category: Pogoryelov, D | + | [[Category: Pogoryelov, D]] |
[[Category: Atp synthesis]] | [[Category: Atp synthesis]] | ||
[[Category: C-ring structure]] | [[Category: C-ring structure]] | ||
Revision as of 22:07, 25 December 2014
Complete ion-coordination structure in the rotor ring of Na-dependent F-ATP synthase
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Categories: Ilyobacter tartaricus | Diederichs, K | Meier, T | Pogoryelov, D | Atp synthesis | C-ring structure | Cell membrane | F1fo-atp synthase rotor | Hydrogen ion transport | Ion coordination and selectivity | Lipid-binding | Membrane protein | Sodium transport | Sodium-motive force | Transmembrane | Transport
