1JRS

HEMIACETAL COMPLEX BETWEEN LEUPEPTIN AND TRYPSIN

1JRS の概要

• エントリーDOI: 10.2210/pdb1jrs/pdb
• 関連するBIRD辞書のPRD_ID: PRD_000216
• 分子名称: TRYPSIN, Leupeptin, CALCIUM ION, ... (4 entities in total)
• 機能のキーワード: hydrolase, serine protease, digestion, pancreas, zymogen, hydrolase (serine protease), hydrolase-hydrolase inhibitor complex, hydrolase/hydrolase inhibitor
• 由来する生物種: Bos taurus (cattle); 詳細
• 細胞内の位置: Secreted, extracellular space: P00760
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 23793.94

構造登録者

Kurinov, I.V.,Harrison, R.W. (登録日: 1996-02-07, 公開日: 1996-10-14, 最終更新日: 2024-11-20)

主引用文献

Kurinov, I.V.,Harrison, R.W.
Two crystal structures of the leupeptin-trypsin complex.
Protein Sci., 5:752-758, 1996

PubMed Abstract: Three-dimensional structures of trypsin with the reversible inhibitor leupeptin have been determined in two different crystal forms. The first structure was determined at 1.7 A resolution with R-factor = 17.7% in the trigonal crystal space group P3(1)21, with unit cell dimensions of a = b = 55.62 A, c = 110.51 A. The second structure was determined at a resolution of 1.8 A with R-factor = 17.5% in the orthorhombic space group P2(1)2(1)2(1), with unit cell dimensions of a = 63.69 A, b = 69.37 A, c = 63.01 A. The overall protein structure is very similar in both crystal forms, with RMS difference for main-chain atoms of 0.27 A. The leupeptin backbone forms four hydrogen bonds with trypsin and a fifth hydrogen bond interaction is mediated by a water molecule. The aldehyde carbonyl of leupeptin forms a covalent bond of 1.42 A length with side-chain oxygen of Ser-195 in the active site. The reaction of trypsin with leupeptin proceeds through the formation of stable tetrahedral complex in which the hemiacetal oxygen atom is pointing out of the oxyanion hole and forming a hydrogen bond with His-57.

PubMed: 8845765

実験手法

X-RAY DIFFRACTION (1.8 Å)