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.

No abstract is available for this paper.

• Publication year

  1998

• Venue

  Journal of Biological Chemistry

• Publication date

  1998-04-10

• Fields of study

  Biology, Chemistry

• Identifiers
  DOI 10.2210/PDB1A5A/PDB
• External record

  Open on Semantic Scholar

• Source metadata

  Semantic Scholar

• No claims are published for this paper.

• No concepts are published for this paper.

• 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.

  1997cited by this paper
• Exchange of K+ or Cs+ for Na+ induces local and long-range changes in the three-dimensional structure of the tryptophan synthase alpha2beta2 complex.

  1996cited by this paper
• X-PLOR Version 3.1: A System for X-ray Crystallography and NMR

  1992cited by this paper
• Reciprocal communication between the lyase and synthase active sites of the tryptophan synthase bienzyme complex.

  1991cited by this paper
• Structural basis for catalysis by tryptophan synthase.

  1991cited by this paper
• Improved methods for building protein models in electron density maps and the location of errors in these models.

  1991cited by this paper
• The alpha subunit of tryptophan synthase. Evidence that aspartic acid 60 is a catalytic residue and that the double alteration of residues 175 and 211 in a second-site revertant restores the proper geometry of the substrate binding site.

  1989cited by this paper
• Three-dimensional structure of the tryptophan synthase alpha 2 beta 2 multienzyme complex from Salmonella typhimurium.

  1988cited by this paper
• Evidence that glutamic acid 49 of tryptophan synthase alpha subunit is a catalytic residue. Inactive mutant proteins substituted at position 49 bind ligands and transmit ligand-dependent to the beta subunit.

  1988cited by this paper
• Site-specific mutagenesis of the alpha subunit of tryptophan synthase from Salmonella typhimurium. Changing arginine 179 to leucine alters the reciprocal transmission of substrate-induced conformational changes between the alpha and beta 2 subunits.

  1987cited by this paper
• Tryptophan synthase alpha subunit glutamic acid 49 is essential for activity. Studies with 19 mutants at position 49.

  1987cited by this paper
• Crystallization and preliminary X-ray crystallographic data of the tryptophan synthase alpha 2 beta 2 complex from Salmonella typhimurium.

  1985cited by this paper
• A genetic and biochemical analysis of second site reversion.

  1963cited by this paper

• Catalytically impaired TrpA subunit of tryptophan synthase from Chlamydia trachomatis is an allosteric regulator of TrpB

  2021cites this paper
• PCR Mutagenesis, Cloning, Expression, Fast Protein Purification Protocols and Crystallization of the Wild Type and Mutant Forms of Tryptophan Synthase.

  2020cites this paper
• Biophysical and computational methods to analyze amino acid interaction networks in proteins

  2016cites this paper
• Amino acid networks in a (β/α)₈ barrel enzyme change during catalytic turnover.

  2014cites this paper
• Long-range interactions in the α subunit of tryptophan synthase help to coordinate ligand binding, catalysis, and substrate channeling.

  2013cites this paper
• In silico identification and characterization of 1-aminocyclopropane-1-carboxylate deaminase from Phytophthora sojae

  2012cites this paper
• Comparative Study of Tryptophan Synthase Beta Chainbetween Pyrococcus furiosus (Archaea) and Salmonella typhimurium (Proteobacteria)

  2011cites this paper
• Large conformational changes in the Escherichia coli tryptophan synthase β2 subunit upon pyridoxal 5′‐phosphate binding

  2010cites this paper
• Tryptophan synthase: the workings of a channeling nanomachine.

  2008cites this paper
• Tryptophan synthase, an allosteric molecular factory.

  2008cites this paper
• Exploring the pyridoxal 5'-phosphate-dependent enzymes.

  2006cites this paper
• On the structural basis of the catalytic mechanism and the regulation of the alpha subunit of tryptophan synthase from Salmonella typhimurium and BX1 from maize, two evolutionarily related enzymes.

  2005cites this paper
• Structural analysis of Pseudomonas 1-aminocyclopropane-1-carboxylate deaminase complexes: insight into the mechanism of a unique pyridoxal-5'-phosphate dependent cyclopropane ring-opening reaction.

  2004cites this paper
• Functional attributes of the phosphate group binding cup of pyridoxal phosphate-dependent enzymes.

  2002cites this paper
• Structure-based design of agrochemicals.

  2002cites this paper
• Tryptophan synthase: a multienzyme complex with an intramolecular tunnel.

  2001cites this paper
• Metabolism of Aromatic Compounds and Nucleic Acid Bases

  2001cites this paper
• Divergent evolution of enzymatic function: mechanistically diverse superfamilies and functionally distinct suprafamilies.

  2001cites this paper
• Novel allosteric effectors of the tryptophan synthase alpha(2)beta(2) complex identified by computer-assisted molecular modeling.

  2000cites this paper
• Mutational Scanning of a Hairpin Loop in the Tryptophan Synthase β-Subunit Implicated in Allostery and Substrate Channeling

  2000influential citation
• The Molecular Basis of Substrate Channeling*

  1999cites this paper
• Common structural elements in the architecture of the cofactor‐binding domains in unrelated families of pyridoxal phosphate‐dependent enzymes

  1999cites this paper
• Structure, evolution and action of vitamin B6-dependent enzymes.

  1998cites this paper
• New results using Laue diffraction and time-resolved crystallography.

  1998cites this paper