2qe7: Difference between revisions
New page: left|200px<br /><applet load="2qe7" size="350" color="white" frame="true" align="right" spinBox="true" caption="2qe7, resolution 3.060Å" /> '''Crystal structure o... |
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==Overview== | ==Overview== | ||
The ATP synthase of the thermoalkaliphilic Bacillus sp. TA2.A1 operates | 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. | ||
==About this Structure== | ==About this Structure== | ||
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[[Category: H(+)-transporting two-sector ATPase]] | [[Category: H(+)-transporting two-sector ATPase]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Cook, G | [[Category: Cook, G M.]] | ||
[[Category: Dimroth, P.]] | [[Category: Dimroth, P.]] | ||
[[Category: Keis, S.]] | [[Category: Keis, S.]] | ||
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[[Category: thermoalkaliphilic]] | [[Category: thermoalkaliphilic]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:38:34 2008'' | ||
Revision as of 19:38, 21 February 2008
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Crystal structure of the f1-atpase from the thermoalkaliphilic bacterium bacillus sp. ta2.a1
OverviewOverview
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.
About this StructureAbout this Structure
2QE7 is a Protein complex structure of sequences from Bacillus sp. t42. Active as H(+)-transporting two-sector ATPase, with EC number 3.6.3.14 Full crystallographic information is available from OCA.
ReferenceReference
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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