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1esc

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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1esc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1esc OCA], [http://www.ebi.ac.uk/pdbsum/1esc PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1esc RCSB]</span>
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[[Category: hydrolase (serine esterase)]]
[[Category: hydrolase (serine esterase)]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:08:36 2008''

Revision as of 17:08, 30 March 2008


PDB ID 1esc

Drag the structure with the mouse to rotate
, resolution 2.1Å
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



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

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