2qe7: Difference between revisions

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[[Image:2qe7.jpg|left|200px]]
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[[Image:2qe7.png|left|200px]]


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{{STRUCTURE_2qe7|  PDB=2qe7  |  SCENE=  }}  
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'''Crystal structure of the f1-atpase from the thermoalkaliphilic bacterium bacillus sp. ta2.a1'''
===Crystal structure of the f1-atpase from the thermoalkaliphilic bacterium bacillus sp. ta2.a1===




==Overview==
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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.
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{{ABSTRACT_PUBMED_17697996}}


==About this Structure==
==About this Structure==
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[[Category: Single particle analysis]]
[[Category: Single particle analysis]]
[[Category: Thermoalkaliphilic]]
[[Category: Thermoalkaliphilic]]
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Revision as of 15:20, 27 July 2008

File:2qe7.png

Template:STRUCTURE 2qe7

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

Template:ABSTRACT PUBMED 17697996

About this Structure

2QE7 is a Protein complex structure of sequences from Bacillus sp. ta2.a1. Full crystallographic information is available from OCA.

Reference

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

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