View source for 1esc

[[Image:1esc.gif|left|200px]]<br /><applet load="1esc" size="450" color="white" frame="true" align="right" spinBox="true" 
caption="1esc, resolution 2.1&Aring;" />
'''THE MOLECULAR MECHANISM OF ENANTIORECOGNITION BY ESTERASES'''<br />

==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 [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]. 

==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://ispc.weizmann.ac.il//pmbin/getpm?pmid=7773790 7773790]
[[Category: Single protein]]
[[Category: Streptomyces scabiei]]
[[Category: Derewenda, U.]]
[[Category: Derewenda, Z.S.]]
[[Category: Patkar, S.]]
[[Category: Schottel, J.L.]]
[[Category: Swenson, L.]]
[[Category: Wei, Y.]]
[[Category: hydrolase (serine esterase)]]

''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 14:16:26 2007''