Structural highlights
3k5b is a 4 chain structure with sequence from Thet8. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
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| NonStd Res: | |
| Gene: | 55981248, TTHA1279 (THET8), 55981245, atpE, TTHA1276, vatE (THET8) |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
[VATE_THET8] Produces ATP from ADP in the presence of a proton gradient across the membrane.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Proton-translocating ATPases are ubiquitous protein complexes that couple ATP catalysis with proton translocation via a rotary catalytic mechanism. The peripheral stalks are essential components that counteract torque generated from proton translocation during ATP synthesis or from ATP hydrolysis during proton pumping. Despite their essential role, the peripheral stalks are the least conserved component of the complexes, differing substantially between subtypes in composition and stoichiometry. We have determined the crystal structure of the peripheral stalk of the A-type ATPase/synthase from Thermus thermophilus consisting of subunits E and G. The structure contains a heterodimeric right-handed coiled coil, a protein fold never observed before. We have fitted this structure into the 23 A resolution EM density of the intact A-ATPase complex, revealing the precise location of the peripheral stalk and new implications for the function and assembly of proton-translocating ATPases.
The structure of the peripheral stalk of Thermus thermophilus H+-ATPase/synthase.,Lee LK, Stewart AG, Donohoe M, Bernal RA, Stock D Nat Struct Mol Biol. 2010 Mar;17(3):373-8. Epub 2010 Feb 21. PMID:20173764[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Lee LK, Stewart AG, Donohoe M, Bernal RA, Stock D. The structure of the peripheral stalk of Thermus thermophilus H+-ATPase/synthase. Nat Struct Mol Biol. 2010 Mar;17(3):373-8. Epub 2010 Feb 21. PMID:20173764 doi:10.1038/nsmb.1761
