1PQA

Trypsin with PMSF at atomic resolution

1PQA の概要

• エントリーDOI: 10.2210/pdb1pqa/pdb
• 関連するPDBエントリー: 1GDN 1GDQ 1PPZ 1PQ5 1PQ7 1PQ8
• 分子名称: Trypsin, SULFATE ION (3 entities in total)
• 機能のキーワード: trypsin, atomic resolution, pmsf, catalysis, hydrolase
• 由来する生物種: Fusarium oxysporum
• 細胞内の位置: Secreted: P35049
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 22546.80

構造登録者

Schmidt, A.,Jelsch, C.,Rypniewski, W.,Lamzin, V.S. (登録日: 2003-06-18, 公開日: 2003-11-11, 最終更新日: 2025-03-26)

主引用文献

Schmidt, A.,Jelsch, C.,Ostergaard, P.,Rypniewski, W.,Lamzin, V.S.
Trypsin Revisited: CRYSTALLOGRAPHY AT (SUB) ATOMIC RESOLUTION AND QUANTUM CHEMISTRY REVEALING DETAILS OF CATALYSIS.
J.Biol.Chem., 278:43357-43362, 2003

PubMed Abstract: A series of crystal structures of trypsin, containing either an autoproteolytic cleaved peptide fragment or a covalently bound inhibitor, were determined at atomic and ultra-high resolution and subjected to ab initio quantum chemical calculations and multipole refinement. Quantum chemical calculations reproduced the observed active site crystal structure with severe deviations from standard stereochemistry and indicated the protonation state of the catalytic residues. Multipole refinement directly revealed the charge distribution in the active site and proved the validity of the ab initio calculations. The combined results confirmed the catalytic function of the active site residues and the two water molecules acting as the nucleophile and the proton donor. The crystal structures represent snapshots from the reaction pathway, close to a tetrahedral intermediate. The de-acylation of trypsin then occurs in true SN2 fashion.

PubMed: 12937176
DOI: 10.1074/jbc.M306944200

実験手法

X-RAY DIFFRACTION (1.23 Å)