2TRM

THE THREE-DIMENSIONAL STRUCTURE OF ASN102 MUTANT OF TRYPSIN. ROLE OF ASP102 IN SERINE PROTEASE CATALYSIS

2TRM の概要

• エントリーDOI: 10.2210/pdb2trm/pdb
• 分子名称: TRYPSIN, CALCIUM ION, BENZAMIDINE, ... (4 entities in total)
• 機能のキーワード: hydrolase (serine proteinase)
• 由来する生物種: Rattus norvegicus (Norway rat)
• 細胞内の位置: Secreted, extracellular space: P00763
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 23974.08

構造登録者

Stroud, R.M.,Finer-Moore, J. (登録日: 1988-04-25, 公開日: 1988-07-16, 最終更新日: 2017-11-29)

主引用文献

Sprang, S.,Standing, T.,Fletterick, R.J.,Stroud, R.M.,Finer-Moore, J.,Xuong, N.H.,Hamlin, R.,Rutter, W.J.,Craik, C.S.
The three-dimensional structure of Asn102 mutant of trypsin: role of Asp102 in serine protease catalysis.
Science, 237:905-909, 1987

PubMed Abstract: The structure of the Asn102 mutant of trypsin was determined in order to distinguish whether the reduced activity of the mutant at neutral pH results from an altered active site conformation or from an inability to stabilize a positive charge on the active site histidine. The active site structure of the Asn102 mutant of trypsin is identical to the native enzyme with respect to the specificity pocket, the oxyanion hole, and the orientation of the nucleophilic serine. The observed decrease in rate results from the loss of nucleophilicity of the active site serine. This decreased nucleophilicity may result from stabilization of a His57 tautomer that is unable to accept the serine hydroxyl proton.

PubMed: 3112942

実験手法

X-RAY DIFFRACTION (2.8 Å)