2xbd

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==Overview==
==Overview==
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BACKGROUND: Many enzymes that digest polysaccharides contain separate, polysaccharide-binding domains. Structures have been previously determined, for a number of cellulose-binding domains (CBDs) from cellulases. RESULTS:, The family IIb xylan-binding domain 1 (XBD1) from Cellulomonas fimi, xylanase D is shown to bind xylan but not cellulose. Its structure is, similar to that of the homologous family IIa CBD from C. fimi Cex, consisting of two four-stranded beta sheets that form a twisted 'beta, sandwich'. The xylan-binding site is a groove made from two tryptophan, residues that stack against the faces of the sugar rings, plus several, hydrogen-bonding polar residues. CONCLUSIONS: The biggest difference, between the family IIa and IIb domains is that in the former the, solvent-exposed ... [[http://ispc.weizmann.ac.il/pmbin/getpm?10425686 (full description)]]
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BACKGROUND: Many enzymes that digest polysaccharides contain separate, polysaccharide-binding domains. Structures have been previously determined, for a number of cellulose-binding domains (CBDs) from cellulases. RESULTS:, The family IIb xylan-binding domain 1 (XBD1) from Cellulomonas fimi, xylanase D is shown to bind xylan but not cellulose. Its structure is, similar to that of the homologous family IIa CBD from C. fimi Cex, consisting of two four-stranded beta sheets that form a twisted 'beta, sandwich'. The xylan-binding site is a groove made from two tryptophan, residues that stack against the faces of the sugar rings, plus several, hydrogen-bonding polar residues. CONCLUSIONS: The biggest difference, between the family IIa and IIb domains is that in the former the, solvent-exposed tryptophan sidechains are coplanar, whereas in the latter, they are perpendicular, forming a twisted binding site. The binding sites, are therefore complementary to the secondary structures of the ligands, cellulose and xylan. XBD1 and CexCBD represent a striking example of two, proteins that have high sequence similarity but a different function.
==About this Structure==
==About this Structure==
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2XBD is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Cellulomonas_fimi Cellulomonas fimi]]. 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: XBD. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2XBD OCA]].
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2XBD is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Cellulomonas_fimi Cellulomonas fimi]. 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: XBD. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2XBD OCA].
==Reference==
==Reference==
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[[Category: xylanase]]
[[Category: xylanase]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 17:44:35 2007''
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 5 13:50:59 2007''

Revision as of 11:45, 5 November 2007


2xbd

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INTERNAL XYLAN BINDING DOMAIN FROM CELLULOMONAS FIMI XYLANASE D, NMR, MINIMIZED AVERAGE STRUCTURE

Overview

BACKGROUND: Many enzymes that digest polysaccharides contain separate, polysaccharide-binding domains. Structures have been previously determined, for a number of cellulose-binding domains (CBDs) from cellulases. RESULTS:, The family IIb xylan-binding domain 1 (XBD1) from Cellulomonas fimi, xylanase D is shown to bind xylan but not cellulose. Its structure is, similar to that of the homologous family IIa CBD from C. fimi Cex, consisting of two four-stranded beta sheets that form a twisted 'beta, sandwich'. The xylan-binding site is a groove made from two tryptophan, residues that stack against the faces of the sugar rings, plus several, hydrogen-bonding polar residues. CONCLUSIONS: The biggest difference, between the family IIa and IIb domains is that in the former the, solvent-exposed tryptophan sidechains are coplanar, whereas in the latter, they are perpendicular, forming a twisted binding site. The binding sites, are therefore complementary to the secondary structures of the ligands, cellulose and xylan. XBD1 and CexCBD represent a striking example of two, proteins that have high sequence similarity but a different function.

About this Structure

2XBD is a Single protein structure of sequence from Cellulomonas fimi. Active as Endo-1,4-beta-xylanase, with EC number 3.2.1.8 Structure known Active Site: XBD. Full crystallographic information is available from OCA.

Reference

A family IIb xylan-binding domain has a similar secondary structure to a homologous family IIa cellulose-binding domain but different ligand specificity., Simpson PJ, Bolam DN, Cooper A, Ciruela A, Hazlewood GP, Gilbert HJ, Williamson MP, Structure. 1999 Jul 15;7(7):853-64. PMID:10425686

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