1uwt: Difference between revisions

Revision as of 12:45, 29 July 2008

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File:1uwt.png

Template:STRUCTURE 1uwt

STRUCTURE OF BETA-GLYCOSIDASE FROM SULFOLOBUS SOLFATARICUS IN COMPLEX WITH D-GALACTOHYDROXIMO-1,5-LACTAMSTRUCTURE OF BETA-GLYCOSIDASE FROM SULFOLOBUS SOLFATARICUS IN COMPLEX WITH D-GALACTOHYDROXIMO-1,5-LACTAM

Template:ABSTRACT PUBMED 15147194

About this StructureAbout this Structure

1UWT is a Single protein structure of sequence from Sulfolobus solfataricus. Full crystallographic information is available from OCA.

ReferenceReference

Structural studies of the beta-glycosidase from Sulfolobus solfataricus in complex with covalently and noncovalently bound inhibitors., Gloster TM, Roberts S, Ducros VM, Perugino G, Rossi M, Hoos R, Moracci M, Vasella A, Davies GJ, Biochemistry. 2004 May 25;43(20):6101-9. PMID:15147194

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OCA

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-'''STRUCTURE OF BETA-GLYCOSIDASE FROM SULFOLOBUS SOLFATARICUS IN COMPLEX WITH D-GALACTOHYDROXIMO-1,5-LACTAM'''
+===STRUCTURE OF BETA-GLYCOSIDASE FROM SULFOLOBUS SOLFATARICUS IN COMPLEX WITH D-GALACTOHYDROXIMO-1,5-LACTAM===
-==Overview==
+<!--
-Transition-state mimicry is increasingly important both to understand enzyme mechanism and to direct the synthesis of putative therapeutic agents. X-ray crystallography is able to provide vital information on the interactions between an enzyme and the potential inhibitor. Here we report the structures, at approximately 2 A resolution, of a family GH1 beta-glycosidase from the hyperthermophilic archaeon Sulfolobus solfataricus, in complex with both covalently (derived from 2-fluoro-glycosides) and noncovalently (hydroximolactam) bound inhibitors. The enzyme has broad specificity, accommodating both gluco- and galacto-configured substrates, and the crystallographic data demonstrate that the only difference in the way these ligands bind lies in the interactions between Gln18, Glu432, and Trp433, and the hydroxyl group at the O3 and O4 positions. Inhibition by the differently configured ligands was also shown to be extremely similar, with K(i) values of 1.04 and 1.08 microM for the gluco and galacto epimers, respectively. The noncovalently bound inhibitors have a trigonal anomeric carbon, adopt a (4)H(3) (half-chair) conformation, and an interaction is formed between O2 and the catalytic nucleophile, all of which contribute to (partial) mimicry of the oxocarbenium-ion-like transition state. The inhibition of the beta-glycosidase from S. solfataricus by hydroximolactams is discussed in light of the emerging work on family GH1 glycosidase inhibition by a spectrum of putative transition-state mimics.
+The line below this paragraph, {{ABSTRACT_PUBMED_15147194}}, adds the Publication Abstract to the page
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 ==About this Structure==
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 [[Category: Glycoside hydrolase]]
 [[Category: Hydrolase]]
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