Cryo-crystallography of a True Substrate, Indole-3-glycerol Phosphate, Bound to a Mutant (αD60N) Tryptophan Synthase α2β2 Complex Reveals the Correct Orientation of Active Site αGlu49
Open Access
- 1 April 1998
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 273 (15) , 8553-8555
- https://doi.org/10.1074/jbc.273.15.8553
Abstract
No abstract availableThis publication has 13 references indexed in Scilit:
- Crystal Structures of a Mutant (βK87T) Tryptophan Synthase α2β2 Complex with Ligands Bound to the Active Sites of the α- and β-Subunits Reveal Ligand-Induced Conformational ChangesBiochemistry, 1997
- Exchange of K+ or Cs+ for Na+ Induces Local and Long-Range Changes in the Three-Dimensional Structure of the Tryptophan Synthase α2β2 ComplexBiochemistry, 1996
- Tryptophan SynthasePublished by Springer Nature ,1995
- Improved methods for building protein models in electron density maps and the location of errors in these modelsActa Crystallographica Section A Foundations of Crystallography, 1991
- Reciprocal communication between the lyase and synthase active sites of the tryptophan synthase bienzyme complexBiochemistry, 1991
- Structural Basis for Catalysis by Tryptophan SynthasePublished by Wiley ,1991
- The α Subunit of Tryptophan SynthaseJournal of Biological Chemistry, 1989
- 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.Journal of Biological Chemistry, 1988
- 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.Journal of Biological Chemistry, 1987
- A Genetic and Biochemical Analysis of Second Site ReversionJournal of Biological Chemistry, 1963