2jie: Difference between revisions
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Revision as of 18:30, 30 October 2007
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BETA-GLUCOSIDASE B FROM BACILLUS POLYMYXA COMPLEXED WITH 2-F-GLUCOSE
OverviewOverview
Bacteria species involved in degradation of cellulosic substrates produce, a variety of enzymes for processing related compounds along the hydrolytic, pathway. Paenibacillus polymyxa encodes two homologous beta-glucosidases, BglA and BglB, presenting different quaternary structures and substrate, specificities. We previously reported the 3D-structure of BglA, which is, highly specific against cellobiose. Here, we present structural analysis, of BglB, a monomeric enzyme that acts as an exo-beta-glucosidase, hydrolyzing cellobiose and cellodextrins of higher degree of, polymerization. The crystal structure of BglB shows that several polar, residues narrow the active site pocket and contour additional subsites., The structure of the BglB-cellotetraose complex confirms these subsites, ... [(full description)]
About this StructureAbout this Structure
2JIE is a [Single protein] structure of sequence from [Paenibacillus polymyxa] with G2F as [ligand]. Active as [Beta-glucosidase], with EC number [3.2.1.21]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].
ReferenceReference
Crystal Structures of Paenibacillus polymyxa beta-Glucosidase B Complexes Reveal the Molecular Basis of Substrate Specificity and Give New Insights into the Catalytic Machinery of Family I Glycosidases., Isorna P, Polaina J, Latorre-Garcia L, Canada FJ, Gonzalez B, Sanz-Aparicio J, J Mol Biol. 2007 Aug 31;371(5):1204-18. Epub 2007 Jun 2. PMID:17585934
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