1esd
From Proteopedia
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|PDB= 1esd |SIZE=350|CAPTION= <scene name='initialview01'>1esd</scene>, resolution 2.3Å | |PDB= 1esd |SIZE=350|CAPTION= <scene name='initialview01'>1esd</scene>, resolution 2.3Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=VXA:METHYLPHOSPHONIC ACID ESTER GROUP'>VXA</scene> | + | |LIGAND= <scene name='pdbligand=VXA:METHYLPHOSPHONIC+ACID+ESTER+GROUP'>VXA</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1esd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1esd OCA], [http://www.ebi.ac.uk/pdbsum/1esd PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1esd RCSB]</span> | ||
}} | }} | ||
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[[Category: Swenson, L.]] | [[Category: Swenson, L.]] | ||
[[Category: Wei, Y.]] | [[Category: Wei, Y.]] | ||
| - | [[Category: VXA]] | ||
[[Category: hydrolase (serine esterase)]] | [[Category: hydrolase (serine esterase)]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:08:39 2008'' |
Revision as of 17:08, 30 March 2008
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| , resolution 2.3Å | |||||||
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| Ligands: | |||||||
| 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
1ESD 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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