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'''THE MOLECULAR MECHANISM OF ENANTIORECOGNITION BY ESTERASES''' | '''THE MOLECULAR MECHANISM OF ENANTIORECOGNITION BY ESTERASES''' | ||
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[[Category: Swenson, L.]] | [[Category: Swenson, L.]] | ||
[[Category: Wei, Y.]] | [[Category: Wei, Y.]] | ||
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Revision as of 12:27, 2 May 2008
THE MOLECULAR MECHANISM OF ENANTIORECOGNITION BY ESTERASES
Overview
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.
About this Structure
1ESC is a Single protein structure of sequence from Streptomyces scabiei. Full crystallographic information is available from OCA.
Reference
A novel variant of the catalytic triad in the Streptomyces scabies esterase., Wei Y, Schottel JL, Derewenda U, Swenson L, Patkar S, Derewenda ZS, Nat Struct Biol. 1995 Mar;2(3):218-23. PMID:7773790 Page seeded by OCA on Fri May 2 15:27:53 2008
