1esc
From Proteopedia
OCA (Talk | contribs)
(New page: 200px<br /><applet load="1esc" size="450" color="white" frame="true" align="right" spinBox="true" caption="1esc, resolution 2.1Å" /> '''THE MOLECULAR MECHANI...)
Next diff →
Revision as of 12:09, 20 November 2007
|
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 Tue Nov 20 14:16:26 2007
