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1esc

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(New page: 200px<br /><applet load="1esc" size="450" color="white" frame="true" align="right" spinBox="true" caption="1esc, resolution 2.1&Aring;" /> '''THE MOLECULAR MECHANI...)
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caption="1esc, resolution 2.1&Aring;" />
'''THE MOLECULAR MECHANISM OF ENANTIORECOGNITION BY ESTERASES'''<br />
'''THE MOLECULAR MECHANISM OF ENANTIORECOGNITION BY ESTERASES'''<br />
==Overview==
==Overview==
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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.
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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==
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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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1ESC OCA].
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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.]]
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[[Category: Derewenda, Z.S.]]
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[[Category: Derewenda, Z S.]]
[[Category: Patkar, S.]]
[[Category: Patkar, S.]]
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[[Category: Schottel, J.L.]]
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[[Category: Schottel, J L.]]
[[Category: Swenson, L.]]
[[Category: Swenson, L.]]
[[Category: Wei, Y.]]
[[Category: Wei, Y.]]
[[Category: hydrolase (serine esterase)]]
[[Category: hydrolase (serine esterase)]]
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''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


1esc, resolution 2.1Å

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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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