1ukr
From Proteopedia
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STRUCTURE OF ENDO-1,4-BETA-XYLANASE C
Overview
The crystal structure of endo-1,4-beta-xylanase I from Aspergillus niger, has been solved by molecular replacement and was refined to 2.4 A, resolution. The final R-factor for all data from 6 to 2.4 A is 17.9%. The, A. niger xylanase has a characteristic fold which is unique for family G, xylanases (root-mean-square deviation = 1.1 A to Trichoderma reesei, xylanase I, which has 53% sequence identity). It consists of a single, domain composed predominantly of beta-strands. Two beta-sheets are twisted, around a deep, long cleft, which is lined with many aromatic amino acid, residues and is large enough to accommodate at least four xylose residues., The two conserved glutamate residues, Glu79 and Glu170, which are likely, to be involved in catalysis, reach into this cleft from opposite sides. A, niger xylanase I is of particular commercial interest because of its low, pH optimum. A model is proposed which explains this low pH optimum, compared to other members of xylanase family G.
About this Structure
1UKR is a Single protein structure of sequence from Aspergillus niger. Active as Endo-1,4-beta-xylanase, with EC number 3.2.1.8 Structure known Active Sites: EA, EB, EC and ED. Full crystallographic information is available from OCA.
Reference
Three-dimensional structure of Endo-1,4-beta-xylanase I from Aspergillus niger: molecular basis for its low pH optimum., Krengel U, Dijkstra BW, J Mol Biol. 1996 Oct 18;263(1):70-8. PMID:8890913
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