1ESC

THE MOLECULAR MECHANISM OF ENANTIORECOGNITION BY ESTERASES

1ESC の概要

• エントリーDOI: 10.2210/pdb1esc/pdb
• 分子名称: ESTERASE (2 entities in total)
• 機能のキーワード: hydrolase (serine esterase)
• 由来する生物種: Streptomyces scabiei
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 33003.75

構造登録者

Wei, Y.,Schottel, J.L.,Derewenda, U.,Swenson, L.,Patkar, S.,Derewenda, Z.S. (登録日: 1994-10-07, 公開日: 1995-10-15, 最終更新日: 2024-10-30)

主引用文献

Wei, Y.,Schottel, J.L.,Derewenda, U.,Swenson, L.,Patkar, S.,Derewenda, Z.S.
A novel variant of the catalytic triad in the Streptomyces scabies esterase.
Nat.Struct.Biol., 2:218-223, 1995

PubMed Abstract: The crystal structure of a novel esterase from Streptomyces scabies, a causal agent of the potato scab disease, was solved at 2.1 A resolution. The tertiary fold of the enzyme is substantially different from that of the alpha/beta hydrolase family and unique among all known hydrolases. The active site contains a dyad of Ser 14 and His 283, closely resembling two of the three components of typical Ser-His-Asp(Glu) triads from other serine hydrolases. Proper orientation of the active site imidazol is maintained by a hydrogen bond between the N delta-H group and a main chain oxygen. Thus, the enzyme constitutes the first known natural variation of the chymotrypsin-like triad in which a carboxylic acid is replaced by a neutral hydrogen-bond acceptor.

PubMed: 7773790
DOI: 10.1038/nsb0395-218

実験手法

X-RAY DIFFRACTION (2.1 Å)