2bfg
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CRYSTAL STRUCTURE OF BETA-XYLOSIDASE (FAM GH39) IN COMPLEX WITH DINITROPHENYL-BETA-XYLOSIDE AND COVALENTLY BOUND XYLOSIDE
OverviewOverview
Beta-D-Xylosidases are glycoside hydrolases that catalyse the release of, xylose units from short xylooligosaccharides and are engaged in the final, breakdown of plant cell-wall hemicelluloses. beta-D-Xylosidases are found, in glycoside hydrolase families 3, 39, 43, 52 and 54. The first crystal, structure of a GH39 beta-xylosidase revealed a multi-domain organization, with the catalytic domain having the canonical (beta/alpha)8 barrel fold., Here, we report the crystal structure of the GH39 Geobacillus, stearothermophilus beta-D-xylosidase, inactivated by a point mutation of, the general acid-base residue E160A, in complex with the chromogenic, substrate molecule 2,5-dinitrophenyl-beta-D-xyloside. Surprisingly, six of, the eight active sites present in the crystallographic asymmetric ... [(full description)]
About this StructureAbout this Structure
2BFG is a [Single protein] structure of sequence from [Bacillus stearothermophilus] with XYS, NA, SO4 and ANX as [ligands]. Active as [[1]], with EC number [3.2.1.37]. Full crystallographic information is available from [OCA].
ReferenceReference
Enzyme-substrate complex structures of a GH39 beta-xylosidase from Geobacillus stearothermophilus., Czjzek M, Ben David A, Bravman T, Shoham G, Henrissat B, Shoham Y, J Mol Biol. 2005 Nov 4;353(4):838-46. Epub 2005 Sep 20. PMID:16212978
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