1bg4
From Proteopedia
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Revision as of 12:50, 30 October 2007
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XYLANASE FROM PENICILLIUM SIMPLICISSIMUM
Overview
Despite its relatively low pH and temperature optimum, the xylanase from, Penicillium simplicissimum performs exceedingly well under conditions of, paper bleaching. We have purified and characterized this enzyme, which, belongs to family 10 of glycosyl hydrolases. Its gene was cloned, and the, sequence of the protein was deduced from the nucleotide sequence. The, xylanase was crystallized from ammonium sulfate at pH 8.4, and X-ray data, were collected at cryo-temperature to a crystallographic resolution of, 1.75 A. The crystal structure was solved by molecular replacement using, the catalytic domain of the Clostridium thermocellum xylanase as a search, model, and refined to a residual of R = 20% (R(free) = 23%) for data, between 10 and 1.75 A. The xylanase folds in an (alpha/beta)8 ... [(full description)]
About this Structure
1BG4 is a [Single protein] structure of sequence from [Penicillium simplicissimum] with NA, TRS and GOL as [ligands]. Active as [Endo-1,4-beta-xylanase], with EC number [3.2.1.8]. Structure known Active Site: ACT. Full crystallographic information is available from [OCA].
Reference
Structure of the xylanase from Penicillium simplicissimum., Schmidt A, Schlacher A, Steiner W, Schwab H, Kratky C, Protein Sci. 1998 Oct;7(10):2081-8. PMID:9792094
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