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,
- 9 March 2002
- journal article
- research article
- Published by American Chemical Society (ACS) in Biochemistry
- Vol. 41 (13) , 4246-4254
- https://doi.org/10.1021/bi015865j
Abstract
Carbohydrate-binding module (CBM) family 13 includes the “R-type” or “ricin superfamily” β-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.Keywords
This publication has 10 references indexed in Scilit:
- Crystal structures of the sugar complexes of Streptomyces olivaceoviridis E-86 xylanase: sugar binding structure of the family 13 carbohydrate binding moduleJournal of Molecular Biology, 2002
- Novel sugar-binding specificity of the type XIII xylan-binding domain of a family F/10 xylanase fromStreptomyces olivaceoviridisE-86FEBS Letters, 2000
- A novel mechanism of xylan binding by a lectin-like module from Streptomyces lividans xylanase 10ABiochemical Journal, 2000
- The Cysteine-Rich Domain of the Macrophage Mannose Receptor Is a Multispecific Lectin That Recognizes Chondroitin Sulfates a and B and Sulfated Oligosaccharides of Blood Group Lewisa and Lewisx Types in Addition to the Sulfated N-Glycans of LutropinThe Journal of Experimental Medicine, 2000
- Novel Galactose-binding Proteins in AnnelidaJournal of Biological Chemistry, 1998
- AMoRe: an automated package for molecular replacementActa Crystallographica Section A Foundations of Crystallography, 1994
- SETOR: Hardware-lighted three-dimensional solid model representations of macromoleculesJournal of Molecular Graphics, 1993
- Molecular structure of Rarobacter faecitabidus protease I. A yeast-lytic serine protease having mannose-binding activity.Journal of Biological Chemistry, 1992
- β-Trefoil foldJournal of Molecular Biology, 1992
- Einige Derivate der CellobioseEuropean Journal of Inorganic Chemistry, 1910