2JET

Crystal structure of a trypsin-like mutant (S189D , A226G) chymotrypsin.

2JET の概要

• エントリーDOI: 10.2210/pdb2jet/pdb
• 関連するPDBエントリー: 1KDQ
• 分子名称: CHYMOTRYPSINOGEN B CHAIN A, CHYMOTRYPSINOGEN B CHAIN B, CHYMOTRYPSINOGEN B CHAIN C, ... (4 entities in total)
• 機能のキーワード: substrate specificity, zymogen, protease, hydrolase, digestion, serine protease, protein engineering
• 由来する生物種: RATTUS NORVEGICUS (RAT); 詳細
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 25679.06

構造登録者

Jelinek, B.,Katona, G.,Fodor, K.,Venekei, I.,Graf, L. (登録日: 2007-01-22, 公開日: 2007-09-18, 最終更新日: 2024-11-06)

主引用文献

Jelinek, B.,Katona, G.,Fodor, K.,Venekei, I.,Graf, L.
The Crystal Structure of a Trypsin-Like Mutant Chymotrypsin: The Role of Position 226 in the Activity and Specificity of S189D Chymotrypsin.
Protein J., 27:79-, 2008

PubMed Abstract: The crystal structure of the S189D+A226G rat chymotrypsin-B mutant has been determined at 2.2 angstroms resolution. This mutant is the most trypsin-like mutant so far in the line of chymotrypsin-to-trypsin conversions, aiming for a more complete understanding of the structural basis of substrate specificity in pancreatic serine proteases. A226G caused significant rearrangements relative to S189D chymotrypsin, allowing an internal conformation of Asp189 which is close to that in trypsin. Serious distortions remain, however, in the activation domain, including zymogen-like features. The pH-profile of activity suggests that the conformation of the S1-site of the mutant is influenced also by the P1 residue of the substrate.

PubMed: 17805946
DOI: 10.1007/S10930-007-9110-3

実験手法

X-RAY DIFFRACTION (2.2 Å)