1v6x
From Proteopedia
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- | [[Image:1v6x.jpg|left|200px]] | + | [[Image:1v6x.jpg|left|200px]] |
- | + | ||
- | '''Crystal Structure Of Xylanase From Streptomyces Olivaceoviridis E-86 Complexed With 3(3)-4-O-methyl-alpha-D-glucuronosyl-xylotriose''' | + | {{Structure |
+ | |PDB= 1v6x |SIZE=350|CAPTION= <scene name='initialview01'>1v6x</scene>, resolution 2.10Å | ||
+ | |SITE= | ||
+ | |LIGAND= <scene name='pdbligand=XYP:BETA-D-XYLOPYRANOSE'>XYP</scene> | ||
+ | |ACTIVITY= [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] | ||
+ | |GENE= | ||
+ | }} | ||
+ | |||
+ | '''Crystal Structure Of Xylanase From Streptomyces Olivaceoviridis E-86 Complexed With 3(3)-4-O-methyl-alpha-D-glucuronosyl-xylotriose''' | ||
+ | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
- | 1V6X is a [ | + | 1V6X is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Streptomyces_olivaceoviridis Streptomyces olivaceoviridis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1V6X OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/14670957 14670957] |
[[Category: Endo-1,4-beta-xylanase]] | [[Category: Endo-1,4-beta-xylanase]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
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[[Category: protein-sugar complex]] | [[Category: protein-sugar complex]] | ||
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:41:39 2008'' |
Revision as of 12:41, 20 March 2008
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, resolution 2.10Å | |||||||
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Ligands: | |||||||
Activity: | Endo-1,4-beta-xylanase, with EC number 3.2.1.8 | ||||||
Coordinates: | save as pdb, mmCIF, xml |
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. 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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