Protein architecture, dynamics and allostery in tryptophan synthase channeling.
The alpha 2 beta 2 form of the tryptophan synthase bienzyme complex catalyses the last two steps in the synthesis of L-tryptophan, consecutive processes that depend on the channeling of the common metabolite, indole, between the sites of the alpha- and beta-subunits through a 25 A-long tunnel. The channeling of indole and the coupling of the activities of the two sites are controlled by allosteric signals derived from covalent transformations at the beta-site that switch the enzyme between an open, low-activity state, to which ligands bind, and a closed, high-activity state, which prevents the escape of indole.
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Department of Biochemistry, University of California, Riverside 92521-0129, USA.
Woehl
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Dunn
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D000494:Allosteric Regulation; D002384:Catalysis; D007211:Indoles / Q000737:chemistry; D011487:Protein Conformation; D014367:Tryptophan Synthase / Q000737:chemistry*
D007211:Indoles; C030374:indole; D014367:Tryptophan Synthase