2jfe
|
THE CRYSTAL STRUCTURE OF HUMAN CYTOSOLIC BETA-GLUCOSIDASE
OverviewOverview
Human cytosolic beta-glucosidase (hCBG) is a xenobiotic-metabolizing, enzyme that hydrolyses certain flavonoid glucosides, with specificity, depending on the aglycone moiety, the type of sugar and the linkage, between them. In this study, the substrate preference of this enzyme was, investigated by mutational analysis, X-ray crystallography and homology, modelling. The crystal structure of hCBG was solved by the molecular, replacement method and refined at 2.7 A resolution. The main-chain fold of, the enzyme belongs to the (beta/alpha)(8) barrel structure, which is, common to family 1 glycoside hydrolases. The active site is located at the, bottom of a pocket (about 16 A deep) formed by large surface loops, surrounding the C termini of the barrel of beta-strands. As for all the, clan of ... [(full description)]
About this StructureAbout this Structure
2JFE is a [Single protein] structure of sequence from [Homo sapiens]. Active as [[1]], with EC number [3.2.1.21]. Full crystallographic information is available from [OCA].
ReferenceReference
The Crystal Structure of Human Cytosolic beta-Glucosidase Unravels the Substrate Aglycone Specificity of a Family 1 Glycoside Hydrolase., Tribolo S, Berrin JG, Kroon PA, Czjzek M, Juge N, J Mol Biol. 2007 Jul 27;370(5):964-75. Epub 2007 May 18. PMID:17555766
Page seeded by OCA on Mon Oct 29 18:14:14 2007