3csm
STRUCTURE OF YEAST CHORISMATE MUTASE WITH BOUND TRP AND AN ENDOOXABICYCLIC INHIBITOR
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OverviewOverview
BACKGROUND: Chorismate mutase (CM) catalyzes the Claisen rearrangement of, chorismate to prephenate, notably the only known enzymatically catalyzed, pericyclic reaction in primary metabolism. Structures of the enzyme in, complex with an endo-oxabicyclic transition state analogue inhibitor, previously determined for Bacillus subtilis and Escherichia coli CM, provide structural insight into the enzyme mechanism. In contrast to these, bacterial CMs, yeast CM is allosterically regulated in two ways:, activation by tryptophan and inhibition by tyrosine. Yeast CM exists in, two allosteric states, R (active) and t (inactive). RESULTS: We have, determined crystal structures of wild-type yeast CM cocrystallized with, tryptophan and an endo-oxabicyclic transition state analogue inhibitor, of, ... [(full description)]
About this StructureAbout this Structure
3CSM is a [Single protein] structure of sequence from [Saccharomyces cerevisiae] with TRP and TSA as [ligands]. Active as [Chorismate mutase], with EC number [5.4.99.5]. Structure known Active Sites: ACB, ACT, REB and REG. Full crystallographic information is available from [OCA].
ReferenceReference
Mechanisms of catalysis and allosteric regulation of yeast chorismate mutase from crystal structures., Strater N, Schnappauf G, Braus G, Lipscomb WN, Structure. 1997 Nov 15;5(11):1437-52. PMID:9384560
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