Distinct Allosteric Pathways in Imidazole Glycerol Phosphate Synthase from Yeast and Bacteria

Author(s):  
Federica Maschietto ◽  
Aria Gheeraert ◽  
Andrea Piazzi ◽  
Victor S. Batista ◽  
Ivan Rivalta
Structure ◽  
2001 ◽  
Vol 9 (10) ◽  
pp. 987-997 ◽  
Author(s):  
Barnali N Chaudhuri ◽  
Stephanie C Lange ◽  
Rebecca S Myers ◽  
Sridar V Chittur ◽  
V.Jo Davisson ◽  
...  

Structure ◽  
2002 ◽  
Vol 10 (2) ◽  
pp. 185-193 ◽  
Author(s):  
Alice Douangamath ◽  
Martina Walker ◽  
Silke Beismann-Driemeyer ◽  
M.Cristina Vega-Fernandez ◽  
Reinhard Sterner ◽  
...  

Biochemistry ◽  
2020 ◽  
Vol 59 (29) ◽  
pp. 2729-2742
Author(s):  
Andrea C. Kneuttinger ◽  
Chitra Rajendran ◽  
Nadja A. Simeth ◽  
Astrid Bruckmann ◽  
Burkhard König ◽  
...  

2021 ◽  
Vol 12 (1) ◽  
Author(s):  
Jan Philip Wurm ◽  
Sihyun Sung ◽  
Andrea Christa Kneuttinger ◽  
Enrico Hupfeld ◽  
Reinhard Sterner ◽  
...  

AbstractImidazole 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.


2001 ◽  
Vol 276 (23) ◽  
pp. 20387-20396 ◽  
Author(s):  
Silke Beismann-Driemeyer ◽  
Reinhard Sterner

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