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000051046 0247_ $$2DOI$$a10.1021/jp054921d
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000051046 084__ $$2WoS$$aChemistry, Physical
000051046 1001_ $$0P:(DE-Juel1)VDB6340$$aAkola, J.$$b0$$uFZJ
000051046 245__ $$aDensity functional calculations of ATP systems II: ATP hydrolysis at the active site of actin
000051046 260__ $$aWashington, DC$$bSoc.$$c2006
000051046 300__ $$a8121 - 8129
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000051046 440_0 $$03694$$aJournal of Physical Chemistry B$$v110$$x1520-6106
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000051046 520__ $$aThe hydrolysis of adenosine 5'-triphosphate (ATP) at the active site of actin has been studied using density functional calculations. The active site is modeled by the triphosphate tail of ATP, an Mg cation, surrounding water molecules, and the nearby protein residues. Four reaction paths have been followed by constraining coordinates that allow phosphate stretching, nucleophilic attack of the catalytic water, and OH(-) formation via water deprotonation. The lowest-energy barrier (21.0 kcal/mol) is obtained for a dissociative reaction where the terminal phosphate breaks on approaching the catalytic water, followed by proton release via a proton wire mechanism. A higher barrier (39.6 kcal/mol) results for an associative reaction path where OH(-) is formed first, with a pentacoordinated phosphorus atom (P-O distances 2.1 A). Stretching the terminal bridging P-O bond results in bond rupture at 2.8 A with an energy barrier of 28.8 kcal/mol. The residues Gln137 and His161 are not important in the reactions, but insight into their roles in vivo has been obtained. The favored coordination of the end products H(2)PO(4)(-) and ADP(3-) includes a hydrogen bond and an O-Mg-O bridge between the phosphates as well as a hydrogen bond between H(2)PO(4)(-) and the Ser14 side chain. The total energy is 2.1 kcal/mol lower than in the initial reactants. Classical simulations of ATP- and ADP.P(i)-actin show few hydrolysis-induced differences in the protein structure, indicating that phosphate migration is necessary for a change in conformation.
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000051046 650_2 $$2MeSH$$aActins: chemistry
000051046 650_2 $$2MeSH$$aAdenosine Triphosphate: chemistry
000051046 650_2 $$2MeSH$$aBinding Sites
000051046 650_2 $$2MeSH$$aHydrogen Bonding
000051046 650_2 $$2MeSH$$aHydrolysis
000051046 650_2 $$2MeSH$$aModels, Molecular
000051046 650_2 $$2MeSH$$aSaccharomyces cerevisiae: chemistry
000051046 650_7 $$00$$2NLM Chemicals$$aActins
000051046 650_7 $$056-65-5$$2NLM Chemicals$$aAdenosine Triphosphate
000051046 650_7 $$2WoSType$$aJ
000051046 7001_ $$0P:(DE-Juel1)VDB60912$$aJones, R. O.$$b1$$uFZJ
000051046 773__ $$0PERI:(DE-600)2006039-7$$a10.1021/jp054921d$$gVol. 110, p. 8121 - 8129$$p8121 - 8129$$q110<8121 - 8129$$tThe @journal of physical chemistry <Washington, DC> / B$$v110$$x1520-6106$$y2006
000051046 8567_ $$uhttp://hdl.handle.net/2128/1437$$uhttp://dx.doi.org/10.1021/jp054921d
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