title: Protein architecture, dynamics and allostery in tryptophan synthase channeling.
abstract: 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.
authors.affiliation: Department of Biochemistry, University of California, Riverside 92521-0129, USA.
authors.forename: P
authors.initials: P
authors.lastname: Pan
authors.forename: E
authors.initials: E
authors.lastname: Woehl
authors.forename: M F
authors.initials: MF
authors.lastname: Dunn
mesh_terms: D000494:Allosteric Regulation; D002384:Catalysis; D007211:Indoles / Q000737:chemistry; D011487:Protein Conformation; D014367:Tryptophan Synthase / Q000737:chemistry*
chemical_list: D007211:Indoles; C030374:indole; D014367:Tryptophan Synthase