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| | {{STRUCTURE_1isw| PDB=1isw | SCENE= }} | | {{STRUCTURE_1isw| PDB=1isw | SCENE= }} |
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| - | '''Crystal structure of xylanase from Streptomyces olivaceoviridis E-86 complexed with xylobiose'''
| + | ===Crystal structure of xylanase from Streptomyces olivaceoviridis E-86 complexed with xylobiose=== |
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| - | ==Overview==
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| - | The family 10 xylanase from Streptomyces olivaceoviridis E-86 contains a (beta/alpha)(8)-barrel as a catalytic domain, a family 13 carbohydrate binding module (CBM) as a xylan binding domain (XBD) and a Gly/Pro-rich linker between them. The crystal structure of this enzyme showed that XBD has three similar subdomains, as indicated by the presence of a triple-repeated sequence, forming a galactose binding lectin fold similar to that found in the ricin toxin B-chain. Comparison with the structure of ricin/lactose complex suggests three potential sugar binding sites in XBD. In order to understand how XBD binds to the xylan chain, we analyzed the sugar-complex structure by the soaking experiment method using the xylooligosaccharides and other sugars. In the catalytic cleft, bound sugars were observed in the xylobiose and xylotriose complex structures. In the XBD, bound sugars were identified in subdomains alpha and gamma in all of the complexes with xylose, xylobiose, xylotriose, glucose, galactose and lactose. XBD binds xylose or xylooligosaccharides at the same sugar binding sites as in the case of the ricin/lactose complex but its binding manner for xylose and xylooligosaccharides is different from the galactose binding mode in ricin, even though XBD binds galactose in the same manner as in the ricin/galactose complex. These different binding modes are utilized efficiently and differently to bind the long substrate to xylanase and ricin-type lectin. XBD can bind any xylose in the xylan backbone, whereas ricin-type lectin recognizes the terminal galactose to sandwich the large sugar chain, even though the two domains have the same family 13 CBM structure. Family 13 CBM has rather loose and broad sugar specificities and is used by some kinds of proteins to bind their target sugars. In such enzyme, XBD binds xylan, and the catalytic domain may assume a flexible position with respect to the XBD/xylan complex, inasmuch as the linker region is unstructured.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_11829503}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 11829503 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_11829503}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Carbohydrate binding domain]] | | [[Category: Carbohydrate binding domain]] |
| | [[Category: Protein-sugar complex]] | | [[Category: Protein-sugar complex]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 20:22:34 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 13:56:52 2008'' |
Revision as of 10:56, 1 July 2008
Template:STRUCTURE 1isw
Crystal structure of xylanase from Streptomyces olivaceoviridis E-86 complexed with xylobiose
Template:ABSTRACT PUBMED 11829503
About this Structure
Full crystallographic information is available from OCA.
Reference
Crystal structures of the sugar complexes of Streptomyces olivaceoviridis E-86 xylanase: sugar binding structure of the family 13 carbohydrate binding module., Fujimoto Z, Kuno A, Kaneko S, Kobayashi H, Kusakabe I, Mizuno H, J Mol Biol. 2002 Feb 8;316(1):65-78. PMID:11829503
Page seeded by OCA on Tue Jul 1 13:56:52 2008
