1bg4
From Proteopedia
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==Overview== | ==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 ... | + | 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 barrel, (TIM-barrel), with additional helices and loops arranged at the "top", forming the active site cleft. In its overall shape, the P. simplicissimum, xylanase structure is similar to other family 10 xylanases, but its active, site cleft is much shallower and wider. This probably accounts for the, differences in catalysis and in the mode of action of this enzyme. Three, glycerol molecules were observed to bind within the active site groove, one of which interacts directly with the catalytic glutamate residues. It, appears that they occupy putative xylose binding subsites. |
==About this Structure== | ==About this Structure== | ||
| - | 1BG4 is a | + | 1BG4 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Penicillium_simplicissimum Penicillium simplicissimum] with NA, TRS and GOL as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Endo-1,4-beta-xylanase Endo-1,4-beta-xylanase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.8 3.2.1.8] Structure known Active Site: ACT. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1BG4 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: tim-barrel]] | [[Category: tim-barrel]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 5 12:45:15 2007'' |
Revision as of 10:39, 5 November 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 barrel, (TIM-barrel), with additional helices and loops arranged at the "top", forming the active site cleft. In its overall shape, the P. simplicissimum, xylanase structure is similar to other family 10 xylanases, but its active, site cleft is much shallower and wider. This probably accounts for the, differences in catalysis and in the mode of action of this enzyme. Three, glycerol molecules were observed to bind within the active site groove, one of which interacts directly with the catalytic glutamate residues. It, appears that they occupy putative xylose binding subsites.
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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