1knm: Difference between revisions

Revision as of 10:36, 2 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1knm.png

Template:STRUCTURE 1knm

Streptomyces lividans Xylan Binding Domain cbm13 in Complex with LactoseStreptomyces lividans Xylan Binding Domain cbm13 in Complex with Lactose

Template:ABSTRACT PUBMED 11914070

About this StructureAbout this Structure

1KNM is a Single protein structure of sequence from Streptomyces lividans. Full crystallographic information is available from OCA.

ReferenceReference

High-resolution crystal structures of the lectin-like xylan binding domain from Streptomyces lividans xylanase 10A with bound substrates reveal a novel mode of xylan binding., Notenboom V, Boraston AB, Williams SJ, Kilburn DG, Rose DR, Biochemistry. 2002 Apr 2;41(13):4246-54. PMID:11914070

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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-'''Streptomyces lividans Xylan Binding Domain cbm13 in Complex with Lactose'''
+===Streptomyces lividans Xylan Binding Domain cbm13 in Complex with Lactose===
-==Overview==
+<!--
-Carbohydrate-binding module (CBM) family 13 includes the "R-type" or "ricin superfamily" beta-trefoil lectins. The C-terminal CBM, CBM13, of xylanase 10A from Streptomyces lividans is a family 13 CBM that is not only structurally similar to the "R-type" lectins but also somewhat functionally similar. The primary function of CBM13 is to bind the polysaccharide xylan, but it retains the ability of the R-type lectins to bind small sugars such as lactose and galactose. The association of CBM13 with xylan appears to involve cooperative and additive participation of three binding pockets in each of the three trefoil domains of CBM13, suggesting a novel mechanism of CBM-xylan interaction. Thus, the interaction of CBM13 with sugars displays considerable plasticity for which we provide a structural rationale. The high-resolution crystal structure of CBM13 was determined by multiple anomalous dispersion from a complex of CBM13 with a brominated ligand. Crystal structures of CBM13 in complex with lactose and xylopentaose revealed two distinct mechanisms of ligand binding. CBM13 has retained its specificity for lactose via Ricin-like binding in all of the three classic trefoil binding pockets. However, CBM13 has the ability to bind either the nonreducing galactosyl moiety or the reducing glucosyl moiety of lactose. The mode of xylopentaose binding suggests adaptive mutations in the trefoil sugar binding scaffold to accommodate internal binding on helical polymers of xylose.
+The line below this paragraph, {{ABSTRACT_PUBMED_11914070}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 11914070 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_11914070}}
 ==About this Structure==
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 [[Category: Lectin-like beta trefoil fold]]
 [[Category: Xylanase a xylan binding domain cbm13]]
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+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul  2 10:36:11 2008''