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000837023 1001_ $$0P:(DE-HGF)0$$aCiupka, Daniel$$b0
000837023 245__ $$aOn the potential alternate binding change mechanism in a dimeric structure of Pyruvate Phosphate Dikinase
000837023 260__ $$aLondon$$bNature Publishing Group$$c2017
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000837023 520__ $$aThe pyruvate phosphate dikinase (PPDK) reaction mechanism is characterized by a distinct spatial separation of reaction centers and large conformational changes involving an opening-closing motion of the nucleotide-binding domain (NBD) and a swiveling motion of the central domain (CD). However, why PPDK is active only in a dimeric form and to what extent an alternate binding change mechanism could underlie this fact has remained elusive. We performed unbiased molecular dynamics simulations, configurational free energy computations, and rigidity analysis to address this question. Our results support the hypothesis that PPDK dimerization influences the opening-closing motion of the NBDs, and that this influence is mediated via the CDs of both chains. Such an influence would be a prerequisite for an alternate binding change mechanism to occur. To the best of our knowledge, this is the first time that a possible explanation has been suggested as to why only dimeric PPDK is active.
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000837023 536__ $$0G:(DE-Juel1)hdd14_20140501$$aInvestigating the swiveling domain mechanism of the Pyruvate phosphate dikinase (PPDK) (hdd14_20140501)$$chdd14_20140501$$fInvestigating the swiveling domain mechanism of the Pyruvate phosphate dikinase (PPDK)$$x1
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000837023 7001_ $$0P:(DE-Juel1)172663$$aGohlke, Holger$$b1$$eCorresponding author
000837023 773__ $$0PERI:(DE-600)2615211-3$$a10.1038/s41598-017-08521-w$$gVol. 7, no. 1, p. 8020$$n1$$p8020$$tScientific reports$$v7$$x2045-2322$$y2017
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