1ese

THE MOLECULAR MECHANISM OF ENANTIORECOGNITION BY ESTERASES

spinqualitylabelsall models 1ese, resolution 2.40Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1ese is a 1 chain structure with sequence from Streptomyces scabiei. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.4Å Ligands: DEP Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function ESTA_STRSC Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed 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. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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