1QQU

CRYSTAL STRUCTURE OF PORCINE BETA TRYPSIN WITH BOUND ACETATE ION

1QQU の概要

• エントリーDOI: 10.2210/pdb1qqu/pdb
• 分子名称: BETA TRYPSIN, CALCIUM ION, ACETATE ION, ... (4 entities in total)
• 機能のキーワード: serine protease, hydrolase
• 由来する生物種: Sus scrofa (pig)
• 細胞内の位置: Secreted, extracellular space: P00761
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 23590.65

構造登録者

Johnson, A.,Gautham, N.,Pattabhi, V. (登録日: 1999-06-09, 公開日: 2000-06-14, 最終更新日: 2024-11-20)

主引用文献

Johnson, A.,Gautham, N.,Pattabhi, V.
Crystal structure at 1.63 A resolution of the native form of porcine beta-trypsin: revealing an acetate ion binding site and functional water network.
Biochim.Biophys.Acta, 1435:7-21, 1999

PubMed Abstract: The active center of a serine protease is the catalytic triad composed of His-57, Ser-195 and Asp-102. The existing crystal structure data on serine proteases have not fully answered a number of fundamental questions relating to the catalytic activity of serine proteases. The new high resolution native porcine beta-trypsin (BPT) structure is aimed at extending the knowledge on the conformation of the active site and the ordered water structure within and around the active site. The crystal structure of BPT has been determined at 1.63 A resolution. An acetate ion bound at the active site of a trypsin molecule by both classical hydrogen bonds and C-HellipsisO hydrogen bonds has been identified for the first time. A large network of water molecules extending from the recognition amino acid Asp-184 to the entry of the active site has been observed in the BPT structure. A detailed comparison with inhibitor complexes and autolysates indicates that the sulfate ion and the acetate ion bind at the same site of the trypsin molecule. The Ser-195 Cbeta-Ogamma-His-57 Nepsilon angle in the catalytic triad of BPT is intermediate between the corresponding values of the complex and native structure due to acetate ion binding. The network of waters from the recognition amino acid to the active site entry is probably the first ever complete picture of functional waters around the active site. Structural comparisons show that the functional waters involved in the binding of small molecule inhibitors and protease inhibitors are distinctly different.

PubMed: 10561533
DOI: 10.1016/S0167-4838(99)00202-2

実験手法

X-RAY DIFFRACTION (1.63 Å)