1esc
From Proteopedia
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| - | [[Image:1esc.gif|left|200px]] | + | [[Image:1esc.gif|left|200px]] |
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| - | '''THE MOLECULAR MECHANISM OF ENANTIORECOGNITION BY ESTERASES''' | + | {{Structure |
| + | |PDB= 1esc |SIZE=350|CAPTION= <scene name='initialview01'>1esc</scene>, resolution 2.1Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
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| + | '''THE MOLECULAR MECHANISM OF ENANTIORECOGNITION BY ESTERASES''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1ESC is a [ | + | 1ESC is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Streptomyces_scabiei Streptomyces scabiei]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ESC OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/7773790 7773790] |
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Streptomyces scabiei]] | [[Category: Streptomyces scabiei]] | ||
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[[Category: hydrolase (serine esterase)]] | [[Category: hydrolase (serine esterase)]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:59:39 2008'' |
Revision as of 08:59, 20 March 2008
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| , resolution 2.1Å | |||||||
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| 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
Page seeded by OCA on Thu Mar 20 10:59:39 2008
