2TYS

CRYSTAL STRUCTURES OF MUTANT (BETAK87T) TRYPTOPHAN SYNTHASE ALPHA2 BETA2 COMPLEX WITH LIGANDS BOUND TO THE ACTIVE SITES OF THE ALPHA AND BETA SUBUNITS REVEAL LIGAND-INDUCED CONFORMATIONAL CHANGES

2TYS の概要

• エントリーDOI: 10.2210/pdb2tys/pdb
• 分子名称: TRYPTOPHAN SYNTHASE, SODIUM ION, [3-HYDROXY-2-METHYL-5-PHOSPHONOOXYMETHYL-PYRIDIN-4-YLMETHYL]-L-TRYPTOPHANE, ... (5 entities in total)
• 機能のキーワード: lyase, carbon-oxygen lyase, tryptophan biosynthesis, pyridoxal phosphate
• 由来する生物種: Salmonella typhimurium; 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 72116.06

構造登録者

Rhee, S.,Parris, K.D.,Hyde, C.C.,Ahmed, S.A.,Miles, E.W.,Davies, D.R. (登録日: 1997-01-08, 公開日: 1997-04-01, 最終更新日: 2024-02-21)

主引用文献

Rhee, S.,Parris, K.D.,Hyde, C.C.,Ahmed, S.A.,Miles, E.W.,Davies, D.R.
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, 36:7664-7680, 1997

PubMed Abstract: 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 3-phosphate (betaK87T-Ser-GP) or indole-3-propanol phosphate (betaK87T-Ser-IPP) bound to the active site of the alpha-subunit. The results further identify the substrate and product binding sites in each subunit and provide insight into conformational changes that occur upon formation of these complexes. The two structures having ligands at the active sites of both alpha- and beta-subunits reveal an important new feature, the ordering of alpha-subunit loop 6 (residues 179-187). Closure of loop 6 isolates the active site of the alpha-subunit from solvent and results in interaction between alphaThr183 and the catalytic residue alphaAsp60. Other conformational differences between the wild type and these two mutant structures include a rigid-body rotation of the alpha-subunit of approximately 5 degrees relative to the beta-subunit and large movements of part of the beta-subunit (residues 93-189) toward the rest of the beta-subunit. Much smaller differences are observed in the betaK87T-Ser structure. Remarkably, binding of tryptophan to the beta active site results in conformational changes very similar to those observed in the betaK87T-Ser-GP and betaK87T-Ser-IPP structures, with exception of the disordered alpha-subunit loop 6. These large-scale changes, the closure of loop 6, and the movements of a small number of side chains in the alpha-beta interaction site provide a structural base for interpreting the allosteric properties of tryptophan synthase.

PubMed: 9201907
DOI: 10.1021/bi9700429

実験手法

X-RAY DIFFRACTION (1.9 Å)