ArticleThe Journal of biological chemistry2009
Portrait of an enzyme, a complete structural analysis of a multimodular {beta}-N-acetylglucosaminidase from Clostridium perfringens.
Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed, 49 citations in OpenAlex.
- Genomic and phenotypic characterization of indigenous violacein-producing Chromobacterium amazonense SAM215 from lake sediment in Bangladesh.Scientific reports · 2026Article
- Unique Fn3-like biosensor in σProtein science : a publication of the Protein Society · 2024Article
- Molecular identification of hyaluronate lyase, not hyaluronidase, as an intrinsic hyaluronan-degrading enzyme in Clostridium perfringens strain ATCC 13124.Scientific reports · 2024Article
- Structural and functional characterization of a multi-domain GH92 α-1,2-mannosidase from Neobacillus novalis.Acta crystallographica. Section D, Structural biology · 2023Article
- Identification and structural analysis of a carbohydrate-binding module specific to alginate, a representative of a new family, CBM96.The Journal of biological chemistry · 2023Article
- Integrative structure determination reveals functional global flexibility for an ultra-multimodular arabinanase.Communications biology · 2022Article
- Cell Surface Xyloglucan Recognition and Hydrolysis by the Human Gut Commensal Bacteroides uniformis.Applied and environmental microbiology · 2022Review
- Structural insights of the enzymes from the chitin utilization locus of Flavobacterium johnsoniae.Scientific reports · 2020Article
- Structural insights of two novel N-acetyl-glucosaminidase enzymes through in silico methods.Turkish journal of chemistry · 2020Article
- Structural and functional analysis of four family 84 glycoside hydrolases from the opportunistic pathogen Clostridium perfringens.Glycobiology · 2019Article
- Rethinking the role of alpha toxin in Clostridium perfringens-associated enteric diseases: a review on bovine necro-haemorrhagic enteritis.Veterinary research · 2017Review
- Diverse modes of galacto-specific carbohydrate recognition by a family 31 glycoside hydrolase from Clostridium perfringens.PloS one · 2017Article
- Structural analysis of a bacterial exo-α-D-N-acetylglucosaminidase in complex with an unusual disaccharide found in class III mucin.Glycobiology · 2012Article
- Carbohydrate recognition by an architecturally complex α-N-acetylglucosaminidase from Clostridium perfringens.PloS one · 2012Article
- A proteomic and cellular analysis of uropods in the pathogen Entamoeba histolytica.PLoS neglected tropical diseases · 2011Article
- Article
- 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
- Structure of a fibronectin type III-like module from Clostridium thermocellum.Acta crystallographica. Section F, Structural biology and crystallization communications · 2010Article
- Screening-based discovery of drug-like O-GlcNAcase inhibitor scaffolds.FEBS letters · 2010Article
- N-acetylglucosamine recognition by a family 32 carbohydrate-binding module from Clostridium perfringens NagH.Journal of molecular biology · 2009Article
Corrections and comments
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Authors and funding
7 authors at 4 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Common features of the extracellular carbohydrate-active virulence factors involved in host-pathogen interactions are their large sizes and modular complexities. This has made them recalcitrant to structural analysis, and therefore our understanding of the significance of modularity in these important proteins is lagging. Clostridium perfringens is a prevalent human pathogen that harbors a wide array of large, extracellular carbohydrate-active enzymes and is an excellent and relevant model system to approach this problem. Here we describe the complete structure of C. perfringens GH84C (NagJ), a 1001-amino acid multimodular homolog of the C. perfringens micro-toxin, which was determined using a combination of small angle x-ray scattering and x-ray crystallography. The resulting structure reveals unprecedented insight into how catalysis, carbohydrate-specific adherence, and the formation of molecular complexes with other enzymes via an ultra-tight protein-protein interaction are spatially coordinated in an enzyme involved in a host-pathogen interaction.
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