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Significance of the Protein Interface Configuration for Allostery in Imidazole Glycerol Phosphate Synthase

Kneuttinger, Andrea C. ; Rajendran, Chitra ; Simeth, Nadja A. ; Bruckmann, Astrid ; König, Burkhard ; Sterner, Reinhard



Abstract

Imidazole glycerol phosphate synthase (ImGPS) from Thermotoga maritima is a model enzyme for studying allostery. The ImGPS complex consists of the cyclase subunit HisF and the glutaminase subunit HisH whose activity is stimulated by substrate binding to HisF in a V-type manner. To investigate the significance of a putative closing hinge motion at the cyclase:glutaminase interface for HisH ...

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