ArticleJournal of molecular biology2009
N-acetylglucosamine recognition by a family 32 carbohydrate-binding module from Clostridium perfringens NagH.
Article in Journal of molecular biology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 44 citations in OpenAlex.
- Gatekeeping Dietary Fiber: The Role of Carbohydrate-Binding Modules in the Human Gut.Journal of microbiology and biotechnology · 2026Review
- Evolutionary analyses of the animal glycosyltransferase family 54 reveals two β1,4-N-acetylglucosaminyltransferase families.iScience · 2025Article
- Repeat modules and N-linked glycans define structure and antigenicity of a critical enterotoxigenic E. coli adhesin.PLoS pathogens · 2024Article
- Repeat modules and N-linked glycans define structure and antigenicity of a critical enterotoxigenicbioRxiv : the preprint server for biology · 2024Article
- Protein engineering of a nanoCLAMP antibody mimetic scaffold as a platform for producing bioprocess-compatible affinity capture ligands.The Journal of biological chemistry · 2023Article
- A bacterial sulfoglycosidase highlights mucin O-glycan breakdown in the gut ecosystem.Nature chemical biology · 2023Article
- Structural and functional characterization of a multi-domain GH92 α-1,2-mannosidase from Neobacillus novalis.Acta crystallographica. Section D, Structural biology · 2023Article
- Qualitative and Quantitative Characterization of Protein-Carbohydrate Interactions by NMR Spectroscopy.Methods in molecular biology (Clifton, N.J.) · 2023Article
- Discovery of a lectin domain that regulates enzyme activity in mouse N-acetylglucosaminyltransferase-IVa (MGAT4A).Communications biology · 2022Article
- Immunoinformatic analysis of the whole proteome for vaccine design: An application toFrontiers in immunology · 2022Article
- Mucin Glycans Signal through the Sensor Kinase RetS to Inhibit Virulence-Associated Traits in Pseudomonas aeruginosa.Current biology : CB · 2021Article
- Structural and functional analysis of four family 84 glycoside hydrolases from the opportunistic pathogen Clostridium perfringens.Glycobiology · 2019Article
- Preliminary studies on development of a novel subunit vaccine targeting Clostridium perfringens mucolytic enzymes for the control of necrotic enteritis in broilers.Poultry science · 2019Article
- Diverse modes of galacto-specific carbohydrate recognition by a family 31 glycoside hydrolase from Clostridium perfringens.PloS one · 2017Article
- Amino Groups of Chitosan Are Crucial for Binding to a Family 32 Carbohydrate Binding Module of a Chitosanase from Paenibacillus elgii.The Journal of biological chemistry · 2016Article
- Unravelling the multiple functions of the architecturally intricate Streptococcus pneumoniae β-galactosidase, BgaA.PLoS pathogens · 2014Article
- Carbohydrate recognition by an architecturally complex α-N-acetylglucosaminidase from Clostridium perfringens.PloS one · 2012Article
- Structural analysis of a putative family 32 carbohydrate-binding module from the Streptococcus pneumoniae enzyme EndoD.Acta crystallographica. Section F, Structural biology and crystallization communications · 2011Article
- Glycoside hydrolase family 89 alpha-N-acetylglucosaminidase from Clostridium perfringens specifically acts on GlcNAc alpha1,4Gal beta1R at the non-reducing terminus of O-glycans in gastric mucin.The Journal of biological chemistry · 2011Article
- Transcriptional responses of Bacillus cereus towards challenges with the polysaccharide chitosan.PloS one · 2011Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Many carbohydrate-active enzymes have complex architectures comprising multiple modules that may be involved in catalysis, carbohydrate binding, or protein-protein interactions. Carbohydrate-binding modules (CBMs) are a common ancillary module whose function is to promote the adherence of the complete enzyme to carbohydrate substrates. CBM family 32 has been proposed to be one of the most diverse CBM families classified to date, yet all of the structurally characterized CBM32s thus far recognize galactose-based ligands. Here, we report a unique binding specificity and mode of ligand binding for a family 32 CBM. NagHCBM32-2 is one of four CBM32 modules in NagH, a family 84 glycoside hydrolase secreted by Clostridium perfringens. NagHCBM32-2 has the beta-sandwich scaffold common to members of the family; however, its specificity for N-acetylglucosamine is unusual among CBMs. X-ray crystallographic analysis of the module at resolutions from 1.45 to 2.0 A and in complex with disaccharides reveals that its mode of sugar recognition is quite different from that observed for galactose-specific CBM32s. This study continues to unravel the diversity of CBMs found in family 32 and how these CBMs might impart the carbohydrate-binding specificity to the extracellular glycoside hydrolases in C. perfringens.
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Registered trials
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.