1AMH

UNCOMPLEXED RAT TRYPSIN MUTANT WITH ASP 189 REPLACED WITH SER (D189S)

1AMH の概要

• エントリーDOI: 10.2210/pdb1amh/pdb
• 分子名称: ANIONIC TRYPSIN, CALCIUM ION (3 entities in total)
• 機能のキーワード: serine protease, activation domain, substrate specificity hydrolase, hydrolase
• 由来する生物種: Rattus rattus (black rat)
• 細胞内の位置: Secreted, extracellular space: P00763
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 47653.81

構造登録者

Szabo, E.,Bocskei, Z.S.,Naray-Szabo, G.,Graf, L. (登録日: 1997-06-17, 公開日: 1997-12-24, 最終更新日: 2024-10-23)

主引用文献

Szabo, E.,Bocskei, Z.,Naray-Szabo, G.,Graf, L.
The three-dimensional structure of Asp189Ser trypsin provides evidence for an inherent structural plasticity of the protease.
Eur.J.Biochem., 263:20-26, 1999

PubMed Abstract: Trypsin mutant Asp189Ser, first described by Gráf et al. [Gráf, L., Jancsó, A., Szilágyi, L., Hegyi, G., Pintér, K., Náray-Szabó, G., Hepp, J., Medzihradszky, K. & Rutter, W.J. (1988) Proc. Natl Acad. Sci. USA 85, 4961-4965] has played an important role in recent studies on the structural basis of substrate-specific catalysis by serine proteases. The present work reports the three-dimensional structure of this mutant crystallized in unliganded form: the first unliganded rat trypsin structure reported. The X-ray structure of the Asp189Ser trypsin mutant in complex with bovine pancreatic trypsin inhibitor is already known. The X-ray structure of free Asp189Ser rat trypsin revealed that the single amino acid mutation at the bottom of the substrate binding pocket of trypsin resulted in extensive structural changes around the mutated site and in dimerization of the mutant, in contrast with the complexed enzyme the structure of which is practically the same as that of wild-type trypsin. The structural rearrangement in the mutant was shown to be restricted to the activation domain region providing further evidence for the allosteric property of this structural-functional unit of the enzyme. This study supports our view that the plasticity of the activation domain may play an important role in the mechanism of substrate-specific serine protease action.

PubMed: 10429182
DOI: 10.1046/j.1432-1327.1999.00452.x

実験手法

X-RAY DIFFRACTION (2.5 Å)