2bnj
From Proteopedia
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THE XYLANASE TA FROM THERMOASCUS AURANTIACUS UTILIZES ARABINOSE DECORATIONS OF XYLAN AS SIGNIFICANT SUBSTRATE SPECIFICITY DETERMINANTS.
Overview
Xylan, which is a key component of the plant cell wall, consists of a, backbone of beta-1,4-linked xylose residues that are decorated with, arabinofuranose, acetyl, 4-O-methyl d-glucuronic acid and ferulate. The, backbone of xylan is hydrolysed by endo-beta1,4-xylanases (xylanases);, however, it is unclear whether the various side-chains of the, polysaccharide are utilized by these enzymes as significant substrate, specificity determinants. To address this question we have determined the, crystal structure of a family 10 xylanase from Thermoascus aurantiacus, in, complex with xylobiose containing an arabinofuranosyl-ferulate side-chain., We show that the distal glycone subsite of the enzyme makes extensive, direct and indirect interactions with the arabinose side-chain, while the, ... [(full description)]
About this Structure
2BNJ is a [Single protein] structure of sequence from [Thermoascus aurantiacus] with FER as [ligand]. Active as [[1]], with EC number [3.2.1.8]. Full crystallographic information is available from [OCA].
Reference
A family 10 Thermoascus aurantiacus xylanase utilizes arabinose decorations of xylan as significant substrate specificity determinants., Vardakou M, Flint J, Christakopoulos P, Lewis RJ, Gilbert HJ, Murray JW, J Mol Biol. 2005 Oct 7;352(5):1060-7. PMID:16140328
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