1AEC

CRYSTAL STRUCTURE OF ACTINIDIN-E-64 COMPLEX+

1AEC の概要

• エントリーDOI: 10.2210/pdb1aec/pdb
• 分子名称: ACTINIDIN, N-[N-[1-HYDROXYCARBOXYETHYL-CARBONYL]LEUCYLAMINO-BUTYL]-GUANIDINE (3 entities in total)
• 機能のキーワード: hydrolase
• 由来する生物種: Actinidia chinensis
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 23930.40

構造登録者

Varughese, K.I. (登録日: 1992-02-05, 公開日: 1993-10-31, 最終更新日: 2024-10-09)

主引用文献

Varughese, K.I.,Su, Y.,Cromwell, D.,Hasnain, S.,Xuong, N.H.
Crystal structure of an actinidin-E-64 complex.
Biochemistry, 31:5172-5176, 1992

PubMed Abstract: E-64, 1-(L-trans-epoxysuccinylleucylamino)-4-guanidinobutane, is a potent and highly selective irreversible inhibitor of cysteine proteases. The crystal structure of a complex of actinidin and E-64 has been determined at 1.86-A resolution by using the difference Fourier method and refined to an R-factor of 14.5%. The electron density map clearly shows that the C2 atom of the E-64 epoxide ring is covalently bonded to the S atom of the active-site cysteine 25. The charged carboxyl group of E-64 forms four H-bonds with the protein and thus may play an important role in favorably positioning the inhibitor molecule for nucleophilic attack by the active-site thiolate anion. The interaction features between E-64 and actinidin are very similar to those seen in the papain-E-64 complex; however, the amino-4-guanidinobutane group orients differently. The crystals of the actinidin-E-64 complex diffracted much better than the papain-E-64 complex, and consequently the present study provides more precise geometrical information on the binding of the inhibitor. Moreover, this study provides yet another confirmation that the binding of E-64 is at the S subsites and not at the S' subsites as has been previously proposed. The original actinidin structure has been revised using the new cDNA sequence information.

PubMed: 1606141
DOI: 10.1021/bi00137a012

実験手法

X-RAY DIFFRACTION (1.86 Å)