2wgm
From Proteopedia
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| - | [[Image:2wgm.png|left|200px]] | ||
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{{STRUCTURE_2wgm| PDB=2wgm | SCENE= }} | {{STRUCTURE_2wgm| PDB=2wgm | SCENE= }} | ||
| + | ===Complete ion-coordination structure in the rotor ring of Na-dependent F-ATP synthase=== | ||
| + | {{ABSTRACT_PUBMED_19500592}} | ||
| - | === | + | ==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] | |
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==About this Structure== | ==About this Structure== | ||
[[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]. | [[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]. | ||
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| - | ==See Also== | ||
| - | *[[ATP synthase|ATP synthase]] | ||
==Reference== | ==Reference== | ||
| - | <ref group="xtra">PMID:019500592</ref><references group="xtra"/> | + | <ref group="xtra">PMID:019500592</ref><references group="xtra"/><references/> |
[[Category: Ilyobacter tartaricus]] | [[Category: Ilyobacter tartaricus]] | ||
[[Category: Diederichs, K.]] | [[Category: Diederichs, K.]] | ||
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[[Category: Atp synthesis]] | [[Category: Atp synthesis]] | ||
[[Category: C-ring structure]] | [[Category: C-ring structure]] | ||
| - | [[Category: Cell inner membrane]] | ||
[[Category: Cell membrane]] | [[Category: Cell membrane]] | ||
[[Category: F1fo-atp synthase rotor]] | [[Category: F1fo-atp synthase rotor]] | ||
[[Category: Hydrogen ion transport]] | [[Category: Hydrogen ion transport]] | ||
| - | [[Category: Ilyobacter tartaricus]] | ||
[[Category: Ion coordination and selectivity]] | [[Category: Ion coordination and selectivity]] | ||
| - | [[Category: Ion transport]] | ||
[[Category: Lipid-binding]] | [[Category: Lipid-binding]] | ||
| - | [[Category: Membrane]] | ||
[[Category: Membrane protein]] | [[Category: Membrane protein]] | ||
[[Category: Sodium transport]] | [[Category: Sodium transport]] | ||
Revision as of 16:25, 19 June 2013
Contents |
Complete ion-coordination structure in the rotor ring of Na-dependent F-ATP synthase
Template:ABSTRACT PUBMED 19500592
Function
[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]
About this Structure
2wgm is a 44 chain structure with sequence from Ilyobacter tartaricus. Full crystallographic information is available from OCA.
Reference
- Meier T, Krah A, Bond PJ, Pogoryelov D, Diederichs K, Faraldo-Gomez JD. Complete ion-coordination structure in the rotor ring of Na+-dependent F-ATP synthases. J Mol Biol. 2009 Aug 14;391(2):498-507. Epub 2009 Jun 3. PMID:19500592 doi:10.1016/j.jmb.2009.05.082
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
