1v6x

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(New page: 200px<br /><applet load="1v6x" size="450" color="white" frame="true" align="right" spinBox="true" caption="1v6x, resolution 2.10&Aring;" /> '''Crystal Structure Of...)
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[[Image:1v6x.jpg|left|200px]]<br /><applet load="1v6x" size="350" color="white" frame="true" align="right" spinBox="true"
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'''Crystal Structure Of Xylanase From Streptomyces Olivaceoviridis E-86 Complexed With 3(3)-4-O-methyl-alpha-D-glucuronosyl-xylotriose'''<br />
'''Crystal Structure Of Xylanase From Streptomyces Olivaceoviridis E-86 Complexed With 3(3)-4-O-methyl-alpha-D-glucuronosyl-xylotriose'''<br />
==Overview==
==Overview==
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The family 10 xylanase from Streptomyces olivaceoviridis E-86 (SoXyn10A), consists of a GH10 catalytic domain, which is joined by a Gly/Pro-rich, linker to a family 13 carbohydrate-binding module (CBM13) that interacts, with xylan. To understand how GH10 xylanases and CBM13 recognize decorated, xylans, the crystal structure of SoXyn10A was determined in complex with, alpha-l-arabinofuranosyl- and, 4-O-methyl-alpha-d-glucuronosyl-xylooligosaccharides. The bound sugars, were observed in the subsites of the catalytic cleft and also in, subdomains alpha and gamma of CBM13. The data reveal that the binding mode, of the oligosaccharides in the active site of the catalytic domain is, entirely consistent with the substrate specificity and, in conjunction, with the accompanying paper, demonstrate that the accommodation of the, side chains in decorated xylans is conserved in GH10 xylanases of SoXyn10A, against arabinoglucuronoxylan. CBM13 was shown to bind xylose or, xylooligosaccharides reversibly by using nonsymmetric sugars as the, ligands. The independent multiple sites in CBM13 may increase the, probability of substrate binding.
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The family 10 xylanase from Streptomyces olivaceoviridis E-86 (SoXyn10A) consists of a GH10 catalytic domain, which is joined by a Gly/Pro-rich linker to a family 13 carbohydrate-binding module (CBM13) that interacts with xylan. To understand how GH10 xylanases and CBM13 recognize decorated xylans, the crystal structure of SoXyn10A was determined in complex with alpha-l-arabinofuranosyl- and 4-O-methyl-alpha-d-glucuronosyl-xylooligosaccharides. The bound sugars were observed in the subsites of the catalytic cleft and also in subdomains alpha and gamma of CBM13. The data reveal that the binding mode of the oligosaccharides in the active site of the catalytic domain is entirely consistent with the substrate specificity and, in conjunction with the accompanying paper, demonstrate that the accommodation of the side chains in decorated xylans is conserved in GH10 xylanases of SoXyn10A against arabinoglucuronoxylan. CBM13 was shown to bind xylose or xylooligosaccharides reversibly by using nonsymmetric sugars as the ligands. The independent multiple sites in CBM13 may increase the probability of substrate binding.
==About this Structure==
==About this Structure==
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1V6X is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Streptomyces_olivaceoviridis Streptomyces olivaceoviridis] with XYP 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] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1V6X OCA].
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1V6X is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Streptomyces_olivaceoviridis Streptomyces olivaceoviridis] with <scene name='pdbligand=XYP:'>XYP</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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1V6X OCA].
==Reference==
==Reference==
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[[Category: protein-sugar complex]]
[[Category: protein-sugar complex]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sun Nov 25 04:39:16 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:32:07 2008''

Revision as of 13:32, 21 February 2008


1v6x, resolution 2.10Å

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Crystal Structure Of Xylanase From Streptomyces Olivaceoviridis E-86 Complexed With 3(3)-4-O-methyl-alpha-D-glucuronosyl-xylotriose

Overview

The family 10 xylanase from Streptomyces olivaceoviridis E-86 (SoXyn10A) consists of a GH10 catalytic domain, which is joined by a Gly/Pro-rich linker to a family 13 carbohydrate-binding module (CBM13) that interacts with xylan. To understand how GH10 xylanases and CBM13 recognize decorated xylans, the crystal structure of SoXyn10A was determined in complex with alpha-l-arabinofuranosyl- and 4-O-methyl-alpha-d-glucuronosyl-xylooligosaccharides. The bound sugars were observed in the subsites of the catalytic cleft and also in subdomains alpha and gamma of CBM13. The data reveal that the binding mode of the oligosaccharides in the active site of the catalytic domain is entirely consistent with the substrate specificity and, in conjunction with the accompanying paper, demonstrate that the accommodation of the side chains in decorated xylans is conserved in GH10 xylanases of SoXyn10A against arabinoglucuronoxylan. CBM13 was shown to bind xylose or xylooligosaccharides reversibly by using nonsymmetric sugars as the ligands. The independent multiple sites in CBM13 may increase the probability of substrate binding.

About this Structure

1V6X is a Protein complex structure of sequences from Streptomyces olivaceoviridis with as ligand. Active as Endo-1,4-beta-xylanase, with EC number 3.2.1.8 Full crystallographic information is available from OCA.

Reference

Crystal structures of decorated xylooligosaccharides bound to a family 10 xylanase from Streptomyces olivaceoviridis E-86., Fujimoto Z, Kaneko S, Kuno A, Kobayashi H, Kusakabe I, Mizuno H, J Biol Chem. 2004 Mar 5;279(10):9606-14. Epub 2003 Dec 11. PMID:14670957

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