Article
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.
Biochemistry - 24 Jun 1997
Rhee S, Parris K D, Hyde C C, Ahmed S A, Miles E W, Davies D R
Abstract excerpt
Three-dimensional structures are reported for a mutant (betaK87T) tryptophan synthase alpha2beta2 complex with either the substrate L-serine (betaK87T-Ser) or product L-tryptophan (betaK87T-Trp) at the active site of the beta-subunit, in which both amino acids form external aldimines with the coenzyme, pyridoxal phosphate. We also present structures with L-serine bound to the beta site and either alpha-glycerol...
Topics
- Binding Sites
- Crystallography, X-Ray
- Molecular Sequence Data
- Mutation
- Protein Conformation
- Salmonella typhimurium
- Tryptophan Synthase