ArticleThe Journal of biological chemistry2013
Understanding how noncatalytic carbohydrate binding modules can display specificity for xyloglucan.
Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed, 37 citations in OpenAlex.
- Structural and functional insights into cellulosomes: masters of plant cell wall degradation.Frontiers in microbiology · 2025Review
- Functional studies on tandem carbohydrate-binding modules of a multimodular enzyme possessing two catalytic domains.Applied and environmental microbiology · 2024Article
- Synergic action of an inserted carbohydrate-binding module in a glycoside hydrolase family 5 endoglucanase.Acta crystallographica. Section D, Structural biology · 2022Article
- Characterization of an Unknown Region Linked to the Glycoside Hydrolase Family 17 β-1,3-Glucanase ofMarine drugs · 2022Article
- Article
- Carbohydrate-binding modules targeting branched polysaccharides: overcoming side-chain recalcitrance in a non-catalytic approach.Bioresources and bioprocessing · 2021Review
- Engineering the conserved and noncatalytic residues of a thermostable β-1,4-endoglucanase to improve specific activity and thermostability.Scientific reports · 2018Article
- Impact of Module-X2 and Carbohydrate Binding Module-3 on the catalytic activity of associated glycoside hydrolases towards plant biomass.Scientific reports · 2017Article
- Stability and Ligand Promiscuity of Type A Carbohydrate-binding Modules Are Illustrated by the Structure ofThe Journal of biological chemistry · 2017Article
- A Comparative Study of Sample Preparation for Staining and Immunodetection of Plant Cell Walls by Light Microscopy.Frontiers in plant science · 2017Article
- Functional and modular analyses of diverse endoglucanases from Ruminococcus albus 8, a specialist plant cell wall degrading bacterium.Scientific reports · 2016Article
- The Dependence of Carbohydrate-Aromatic Interaction Strengths on the Structure of the Carbohydrate.Journal of the American Chemical Society · 2016Article
- Article
- Vina-Carb: Improving Glycosidic Angles during Carbohydrate Docking.Journal of chemical theory and computation · 2016Article
- Identification of a novel family of carbohydrate-binding modules with broad ligand specificity.Scientific reports · 2016Article
- Crystallization, neutron data collection, initial structure refinement and analysis of a xyloglucan heptamer bound to an engineered carbohydrate-binding module from xylanase.Acta crystallographica. Section F, Structural biology communications · 2015Article
- Cloning, purification, crystallization and preliminary X-ray studies of a carbohydrate-binding module (CBM_E1) derived from sugarcane soil metagenome.Acta crystallographica. Section F, Structural biology communications · 2014Article
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Authors and funding
12 authors at 2 institutions in 1 country.
Funding
Abstract
Plant biomass is central to the carbon cycle and to environmentally sustainable industries exemplified by the biofuel sector. Plant cell wall degrading enzymes generally contain noncatalytic carbohydrate binding modules (CBMs) that fulfil a targeting function, which enhances catalysis. CBMs that bind β-glucan chains often display broad specificity recognizing β1,4-glucans (cellulose), β1,3-β1,4-mixed linked glucans and xyloglucan, a β1,4-glucan decorated with α1,6-xylose residues, by targeting structures common to the three polysaccharides. Thus, CBMs that recognize xyloglucan target the β1,4-glucan backbone and only accommodate the xylose decorations. Here we show that two closely related CBMs, CBM65A and CBM65B, derived from EcCel5A, a Eubacterium cellulosolvens endoglucanase, bind to a range of β-glucans but, uniquely, display significant preference for xyloglucan. The structures of the two CBMs reveal a β-sandwich fold. The ligand binding site comprises the β-sheet that forms the concave surface of the proteins. Binding to the backbone chains of β-glucans is mediated primarily by five aromatic residues that also make hydrophobic interactions with the xylose side chains of xyloglucan, conferring the distinctive specificity of the CBMs for the decorated polysaccharide. Significantly, and in contrast to other CBMs that recognize β-glucans, CBM65A utilizes different polar residues to bind cellulose and mixed linked glucans. Thus, Gln(106) is central to cellulose recognition, but is not required for binding to mixed linked glucans. This report reveals the mechanism by which β-glucan-specific CBMs can distinguish between linear and mixed linked glucans, and show how these CBMs can exploit an extensive hydrophobic platform to target the side chains of decorated β-glucans.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.