1ur2
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(New page: 200px<br /> <applet load="1ur2" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ur2, resolution 1.60Å" /> '''XYLANASE XYN10B MUT...)
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Revision as of 18:29, 29 October 2007
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XYLANASE XYN10B MUTANT (E262S) FROM CELLVIBRIO MIXTUS IN COMPLEX WITH ARABINOFURANOSE ALPHA 1,3 LINKED TO XYLOTRIOSE
Overview
Endo-beta-1,4-xylanases (xylanases), which cleave beta-1,4 glycosidic, bonds in the xylan backbone, are important components of the repertoire of, enzymes that catalyze plant cell wall degradation. The mechanism by which, these enzymes are able to hydrolyze a range of decorated xylans remains, unclear. Here we reveal the three-dimensional structure, determined by, x-ray crystallography, and the catalytic properties of the Cellvibrio, mixtus enzyme Xyn10B (CmXyn10B), the most active GH10 xylanase described, to date. The crystal structure of the enzyme in complex with xylopentaose, reveals that at the +1 subsite the xylose moiety is sandwiched between, hydrophobic residues, which is likely to mediate tighter binding than in, other GH10 xylanases. The crystal structure of the xylanase in ... [(full description)]
About this Structure
1UR2 is a [Single protein] structure of sequence from [Cellvibrio mixtus] with CL and MG as [ligands]. Active as [[1]], with EC number [3.2.1.8]. Full crystallographic information is available from [OCA].
Reference
The mechanisms by which family 10 glycoside hydrolases bind decorated substrates., Pell G, Taylor EJ, Gloster TM, Turkenburg JP, Fontes CM, Ferreira LM, Nagy T, Clark SJ, Davies GJ, Gilbert HJ, J Biol Chem. 2004 Mar 5;279(10):9597-605. Epub 2003 Dec 10. PMID:14668328
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