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Analysis of five crystal structures of dimeric yeast chorismate mutase include a T-state bound to the allosteric inhibitor Tyr, two R-state mutants and two super-R wild- type structures bound to the transition state inhibitor plus either Tyr or the allosteric activator Trp. Relative rotations of one subunit relative to the other are 0' (reference) for T, 15' for R and 22' for super-R states. A well defined pathway for conformational changes occurs from the active site to the subunit interface. Comparisons are made with other allosteric enzymes. YEAST CHORISMATE MUTASE (YCM)

Yeast chorismate and other allosteric enzymes