2bnj: Difference between revisions
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[[Image:2bnj.gif|left|200px]]<br /><applet load="2bnj" size=" | [[Image:2bnj.gif|left|200px]]<br /><applet load="2bnj" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="2bnj, resolution 1.600Å" /> | caption="2bnj, resolution 1.600Å" /> | ||
'''THE XYLANASE TA FROM THERMOASCUS AURANTIACUS UTILIZES ARABINOSE DECORATIONS OF XYLAN AS SIGNIFICANT SUBSTRATE SPECIFICITY DETERMINANTS.'''<br /> | '''THE XYLANASE TA FROM THERMOASCUS AURANTIACUS UTILIZES ARABINOSE DECORATIONS OF XYLAN AS SIGNIFICANT SUBSTRATE SPECIFICITY DETERMINANTS.'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
2BNJ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermoascus_aurantiacus Thermoascus aurantiacus] with FER as [http://en.wikipedia.org/wiki/ligand ligand]. 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] Known structural/functional Site: <scene name='pdbsite=AC1:Fer Binding Site For Chain A'>AC1</scene>. Full crystallographic information is available from [http:// | 2BNJ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermoascus_aurantiacus Thermoascus aurantiacus] with <scene name='pdbligand=FER:'>FER</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. 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] Known structural/functional Site: <scene name='pdbsite=AC1:Fer+Binding+Site+For+Chain+A'>AC1</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BNJ OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: xylanase]] | [[Category: xylanase]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb 3 10:26:05 2008'' | ||
Revision as of 11:26, 3 February 2008
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THE XYLANASE TA FROM THERMOASCUS AURANTIACUS UTILIZES ARABINOSE DECORATIONS OF XYLAN AS SIGNIFICANT SUBSTRATE SPECIFICITY DETERMINANTS.
OverviewOverview
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, ferulate moiety is solvent-exposed. Consistent with the 3D structural, data, the xylanase displays fourfold more activity against xylotriose in, which the non-reducing moiety is linked to an arabinose side-chain, compared to the undecorated form of the oligosacchairde. These data, indicate that the sugar decorations of xylans in the T.aurantiacus family, 10 xylanase, rather than simply being accommodated, can be significant, substrate specificity determinants.
About this StructureAbout this Structure
2BNJ is a Single protein structure of sequence from Thermoascus aurantiacus with as ligand. Active as Endo-1,4-beta-xylanase, with EC number 3.2.1.8 Known structural/functional Site: . Full crystallographic information is available from OCA.
ReferenceReference
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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