1wu4
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(New page: 200px<br /><applet load="1wu4" size="450" color="white" frame="true" align="right" spinBox="true" caption="1wu4, resolution 1.35Å" /> '''Crystal structure of...)
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Revision as of 22:36, 24 November 2007
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Crystal structure of reducing-end-xylose releasing exo-oligoxylanase
Overview
Reducing end xylose-releasing exo-oligoxylanase from Bacillus halodurans, C-125 (Rex) hydrolyzes xylooligosaccharides whose degree of polymerization, is greater than or equal to 3, releasing the xylose unit at the reducing, end. It is a unique exo-type glycoside hydrolase that recognizes the, xylose unit at the reducing end in a very strict manner, even, discriminating the beta-anomeric hydroxyl configuration from the, alpha-anomer or 1-deoxyxylose. We have determined the crystal structures, of Rex in unliganded and complex forms at 1.35-2.20-A resolution and, revealed the structural aspects of its three subsites ranging from -2 to, +1. The structure of Rex was compared with those of endo-type enzymes in, glycoside hydrolase subfamily 8a (GH-8a). The catalytic machinery of Rex, is basically conserved with other GH-8a enzymes. However, subsite +2 is, blocked by a barrier formed by a kink in the loop before helix alpha10., His-319 in this loop forms a direct hydrogen bond with the beta-hydroxyl, of xylose at subsite +1, contributing to the specific recognition of, anomers at the reducing end.
About this Structure
1WU4 is a Single protein structure of sequence from Bacteria with NI and GOL as ligands. Active as Oligosaccharide reducing-end xylanase, with EC number 3.2.1.156 Full crystallographic information is available from OCA.
Reference
Structural basis for the specificity of the reducing end xylose-releasing exo-oligoxylanase from Bacillus halodurans C-125., Fushinobu S, Hidaka M, Honda Y, Wakagi T, Shoun H, Kitaoka M, J Biol Chem. 2005 Apr 29;280(17):17180-6. Epub 2005 Feb 17. PMID:15718242
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