Structural highlights
Function
[Q71CG2_9BACI] Produces ATP from ADP in the presence of a proton gradient across the membrane (By similarity).[HAMAP-Rule:MF_00530] [Q71CG5_9BACI] Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit (By similarity).[HAMAP-Rule:MF_01346] [Q71CG4_9BACI] Produces ATP from ADP in the presence of a proton gradient across the membrane. The gamma chain is believed to be important in regulating ATPase activity and the flow of protons through the CF(0) complex (By similarity).[HAMAP-Rule:MF_00815][RuleBase:RU004001][SAAS:SAAS023632_004_025650] [Q71CG3_9BACI] Produces ATP from ADP in the presence of a proton gradient across the membrane. The catalytic sites are hosted primarily by the beta subunits (By similarity).[HAMAP-Rule:MF_01347]
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
The ATP synthase of the thermoalkaliphilic Bacillus sp. TA2.A1 operates exclusively in ATP synthesis direction. In the crystal structure of the nucleotide-free alpha(3)beta(3)gamma epsilon subcomplex (TA2F(1)) at 3.1 A resolution, all three beta subunits adopt the open beta(E) conformation. The structure shows salt bridges between the helix-turn-helix motif of the C-terminal domain of the beta(E) subunit (residues Asp372 and Asp375) and the N-terminal helix of the gamma subunit (residues Arg9 and Arg10). These electrostatic forces pull the gamma shaft out of the rotational center and impede rotation through steric interference with the beta(E) subunit. Replacement of Arg9 and Arg10 with glutamines eliminates the salt bridges and results in an activation of ATP hydrolysis activity, suggesting that these salt bridges prevent the native enzyme from rotating in ATP hydrolysis direction. A similar bending of the gamma shaft as in the TA2F(1) structure was observed by single-particle analysis of the TA2F(1)F(o) holoenzyme.
The structural basis for unidirectional rotation of thermoalkaliphilic F1-ATPase.,Stocker A, Keis S, Vonck J, Cook GM, Dimroth P Structure. 2007 Aug;15(8):904-14. PMID:17697996[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Stocker A, Keis S, Vonck J, Cook GM, Dimroth P. The structural basis for unidirectional rotation of thermoalkaliphilic F1-ATPase. Structure. 2007 Aug;15(8):904-14. PMID:17697996 doi:http://dx.doi.org/10.1016/j.str.2007.06.009
