1GBA

ALPHA-LYTIC PROTEASE WITH MET 190 REPLACED BY ALA AND GLY 216 REPLACED BY ALA

1GBA の概要

• エントリーDOI: 10.2210/pdb1gba/pdb
• 分子名称: ALPHA-LYTIC PROTEASE, SULFATE ION (3 entities in total)
• 機能のキーワード: active-site mutation, hydrolase (serine proteinase)
• 由来する生物種: Lysobacter enzymogenes
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 20021.17

構造登録者

Mace, J.E.,Agard, D.A. (登録日: 1995-09-06, 公開日: 1996-01-29, 最終更新日: 2024-10-23)

主引用文献

Mace, J.E.,Agard, D.A.
Kinetic and structural characterization of mutations of glycine 216 in alpha-lytic protease: a new target for engineering substrate specificity.
J.Mol.Biol., 254:720-736, 1995

PubMed Abstract: Gly216 in the active site of the broadly specific MA190 mutant of alpha-lytic protease has been found to be remarkably tolerant of amino acid substitutions. Side-chains as large as Trp can be accommodated within the substrate-binding pocket without abolishing catalysis, and have major effects upon the substrate specificity of the enzyme. Kinetic characterization of eleven enzymatically active mutants against a panel of eight substrates clearly revealed the functional consequences of the substitutions at position 216. To understand better the structural basis for their altered specificity, the GA216 + MA190 and GL216 + MA190 mutants have been crystallized both with and without a representative series of peptide boronic acid transition-state analog inhibitors. An empirical description and non-parametric statistical analysis of structural variation among these enzyme: inhibitor complexes is presented. The roles of active site plasticity and dynamics in alpha-lytic protease function and substrate preference are also addressed. The results strongly suggest that substrate specificity determination in alpha-lytic protease is a distributed property of the active site and substrate molecule.

PubMed: 7500345
DOI: 10.1006/jmbi.1995.0650

実験手法

X-RAY DIFFRACTION (2.15 Å)