1ESB

DIRECT STRUCTURE OBSERVATION OF AN ACYL-ENZYME INTERMEDIATE IN THE HYDROLYSIS OF AN ESTER SUBSTRATE BY ELASTASE

1ESB の概要

• エントリーDOI: 10.2210/pdb1esb/pdb
• 分子名称: PORCINE PANCREATIC ELASTASE, N-[(BENZYLOXY)CARBONYL]-L-ALANINE, CALCIUM ION, ... (5 entities in total)
• 機能のキーワード: hydrolase, serine proteinase
• 由来する生物種: Sus scrofa (pig)
• 細胞内の位置: Secreted: P00772
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 26287.40

構造登録者

Ding, X.,Rasmussen, B.,Petsko, G.A.,Ringe, D. (登録日: 1994-02-04, 公開日: 1994-04-30, 最終更新日: 2024-10-30)

主引用文献

Ding, X.,Rasmussen, B.F.,Petsko, G.A.,Ringe, D.
Direct structural observation of an acyl-enzyme intermediate in the hydrolysis of an ester substrate by elastase.
Biochemistry, 33:9285-9293, 1994

PubMed Abstract: The method of X-ray crystallographic cryoenzymology has been used to determine the crystal structure of a kinetically significant species on the reaction pathway of a crystalline enzyme. The structure of a specific acyl-enzyme intermediate in the elastase-catalyzed hydrolysis of the N-carbobenzoxy-L-alanine p-nitrophenyl ester has been determined and refined against X-ray diffraction data at 2.3-A resolution. The difference Fourier electron density map clearly shows electron density for the trapped acyl-enzyme. The acyl-enzyme was formed at -26 degrees C and was stabilized at -55 degrees C during data collection, taking advantage of the glass transition in protein dynamics that occurs at around -50 degrees C.

PubMed: 8049229
DOI: 10.1021/bi00197a032

実験手法

X-RAY DIFFRACTION (2.3 Å)