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000459161 1001_ $$00000-0003-0985-7273$$aWurm, Jan Philip$$b0
000459161 245__ $$aMolecular basis for the allosteric activation mechanism of the heterodimeric imidazole glycerol phosphate synthase complex
000459161 260__ $$a[London]$$bNature Publishing Group UK$$c2021
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000459161 520__ $$aImidazole glycerol phosphate synthase (HisFH) is a heterodimeric bienzyme complex operating at a central branch point of metabolism. HisFH is responsible for the HisH-catalyzed hydrolysis of glutamine to glutamate and ammonia, which is then used for a cyclase reaction by HisF. The HisFH complex is allosterically regulated but the underlying mechanism is not well understood. Here, we elucidate the molecular basis of the long range, allosteric activation of HisFH. We establish that the catalytically active HisFH conformation is only formed when the substrates of both HisH and HisF are bound. We show that in this conformation an oxyanion hole in the HisH active site is established, which rationalizes the observed 4500-fold allosteric activation compared to the inactive conformation. In solution, the inactive and active conformations are in a dynamic equilibrium and the HisFH turnover rates correlate with the population of the active conformation, which is in accordance with the ensemble model of allostery.
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000459161 7001_ $$0P:(DE-HGF)0$$aSung, Sihyun$$b1
000459161 7001_ $$aKneuttinger, Andrea Christa$$b2
000459161 7001_ $$aHupfeld, Enrico$$b3
000459161 7001_ $$aSterner, Reinhard$$b4
000459161 7001_ $$0P:(DE-HGF)0$$aWilmanns, Matthias$$b5$$eCorresponding author
000459161 7001_ $$0P:(DE-HGF)0$$aSprangers, Remco$$b6$$eCorresponding author
000459161 773__ $$0PERI:(DE-600)2553671-0$$a10.1038/s41467-021-22968-6$$gVol. 12, no. 1, p. 2748$$n1$$p2748$$tNature Communications$$v12$$x2041-1723$$y2021
000459161 8564_ $$uhttps://www.nature.com/articles/s41467-021-22968-6
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