Crystal structure of the beta Ser178--> Pro mutant of tryptophan synthase. A "knock-out" allosteric enzyme (Q27637096)

1

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Andrea Mozzarelli

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Anna Marabotti

object named as

Anna Marabotti

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author name string

Petra Herde

Journal of Biological Chemistry

3

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language of work or name

English

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publication date

22 March 2002

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published in

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volume

277

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issue

12

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page(s)

10653-60

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cites work

The tryptophan synthase bienzyme complex transfers indole between the alpha- and beta-sites via a 25-30 A long tunnel

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Reciprocal communication between the lyase and synthase active sites of the tryptophan synthase bienzyme complex.

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Monovalent cations affect dynamic and functional properties of the tryptophan synthase alpha 2 beta 2 complex.

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Allosteric interactions coordinate catalytic activity between successive metabolic enzymes in the tryptophan synthase bienzyme complex

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beta-Site covalent reactions trigger transitions between open and closed conformations of the tryptophan synthase bienzyme complex

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Crystal structures of a mutant (betaK87T) tryptophan synthase alpha2beta2 complex with ligands bound to the active sites of the alpha- and beta-subunits reveal ligand-induced conformational changes

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Loop closure and intersubunit communication in tryptophan synthase

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Characterization of the functional role of a flexible loop in the alpha-subunit of tryptophan synthase from Salmonella typhimurium by rapid-scanning, stopped-flow spectroscopy and site-directed mutagenesis

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Allosteric communication of tryptophan synthase. Functional and regulatory properties of the beta S178P mutant

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Beta D305A mutant of tryptophan synthase shows strongly perturbed allosteric regulation and substrate specificity

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Novel allosteric effectors of the tryptophan synthase alpha(2)beta(2) complex identified by computer-assisted molecular modeling

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Crystal structures of a new class of allosteric effectors complexed to tryptophan synthase

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Crystal structure of wild-type tryptophan synthase complexed with the natural substrate indole-3-glycerol phosphate

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Exchange of K+ or Cs+ for Na+ induces local and long-range changes in the three-dimensional structure of the tryptophan synthase alpha2beta2 complex

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Cryocrystallography and microspectrophotometry of a mutant (alpha D60N) tryptophan synthase alpha 2 beta 2 complex reveals allosteric roles of alpha Asp60

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Cryo-crystallography of a true substrate, indole-3-glycerol phosphate, bound to a mutant (alphaD60N) tryptophan synthase alpha2beta2 complex reveals the correct orientation of active site alphaGlu49

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Crystallographic studies of phosphonate-based alpha-reaction transition-state analogues complexed to tryptophan synthase

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Roles of hydrogen bonding residues in the interaction between the alpha and beta subunits in the tryptophan synthase complex. Asn-104 of the alpha subunit is especially important.

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Substitution of glutamic acid 109 by aspartic acid alters the substrate specificity and catalytic activity of the beta-subunit in the tryptophan synthase bienzyme complex from Salmonella typhimurium

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Mutations in the contact region between the alpha and beta subunits of tryptophan synthase alter subunit interaction and intersubunit communication

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Monovalent cations partially repair a conformational defect in a mutant tryptophan synthase alpha 2 beta 2 complex (beta-E109A)

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