2QE7

Crystal structure of the f1-atpase from the thermoalkaliphilic bacterium bacillus sp. ta2.a1

Summary for 2QE7

• Entry DOI: 10.2210/pdb2qe7/pdb
• Related: 1JNV 1SKY
• Descriptor: ATP synthase subunit alpha, ATP synthase subunit beta, ATP synthase subunit gamma, ... (4 entities in total)
• Functional Keywords: blockage of atp hydrolysis, f1-atpase, atp synthase, single particle analysis, thermoalkaliphilic, hydrolase
• Biological source: Bacillus sp.; More
• Cellular location: Cell membrane; Peripheral membrane protein (By similarity): Q71CG5 Q71CG3 Q71CG4 Q71CG2
• Total number of polymer chains: 8
• Total formula weight: 362763.77

Authors

Stocker, A.,Keis, S.,Vonck, J.,Cook, G.M.,Dimroth, P. (deposition date: 2007-06-25, release date: 2007-08-21, Last modification date: 2023-08-30)

Primary citation

Stocker, A.,Keis, S.,Vonck, J.,Cook, G.M.,Dimroth, P.
The Structural Basis for Unidirectional Rotation of Thermoalkaliphilic F(1)-ATPase.
Structure, 15:904-914, 2007

PubMed Abstract: 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.

PubMed: 17697996
DOI: 10.1016/j.str.2007.06.009

Experimental method

X-RAY DIFFRACTION (3.06 Å)