1esc
From Proteopedia
(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...) |
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| - | [[Image:1esc.gif|left|200px]]<br /><applet load="1esc" size=" | + | [[Image:1esc.gif|left|200px]]<br /><applet load="1esc" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1esc, resolution 2.1Å" /> | caption="1esc, resolution 2.1Å" /> | ||
'''THE MOLECULAR MECHANISM OF ENANTIORECOGNITION BY ESTERASES'''<br /> | '''THE MOLECULAR MECHANISM OF ENANTIORECOGNITION BY ESTERASES'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The crystal structure of a novel esterase from Streptomyces scabies, a | + | 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== | ==About this Structure== | ||
| - | 1ESC is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Streptomyces_scabiei Streptomyces scabiei]. Full crystallographic information is available from [http:// | + | 1ESC is a [http://en.wikipedia.org/wiki/Single_protein 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== | ||
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[[Category: Streptomyces scabiei]] | [[Category: Streptomyces scabiei]] | ||
[[Category: Derewenda, U.]] | [[Category: Derewenda, U.]] | ||
| - | [[Category: Derewenda, Z | + | [[Category: Derewenda, Z S.]] |
[[Category: Patkar, S.]] | [[Category: Patkar, S.]] | ||
| - | [[Category: Schottel, J | + | [[Category: Schottel, J L.]] |
[[Category: Swenson, L.]] | [[Category: Swenson, L.]] | ||
[[Category: Wei, Y.]] | [[Category: Wei, Y.]] | ||
[[Category: hydrolase (serine esterase)]] | [[Category: hydrolase (serine esterase)]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:30:57 2008'' |
Revision as of 10:31, 21 February 2008
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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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