Portrait of an Enzyme, a Complete Structural Analysis of a Multimodular β-N-Acetylglucosaminidase from Clostridium perfringens

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 importa...

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Bibliographic Details
Published in:The Journal of biological chemistry 2009-04, Vol.284 (15), p.9876-9884
Main Authors: Ficko-Blean, Elizabeth, Gregg, Katie J., Adams, Jarrett J., Hehemann, Jan-Hendrik, Czjzek, Mirjam, Smith, Steven P., Boraston, Alisdair B.
Format: Article
Language:English
Subjects:
BASIC BIOLOGICAL SCIENCES
CATALYSIS
CLOSTRIDIUM PERFRINGENS
COMPLEXES
CRYSTALLOGRAPHY
ENZYMES
GENERAL AND MISCELLANEOUS//MATHEMATICS, COMPUTING, AND INFORMATION SCIENCE
HARBORS
HUMAN POPULATIONS
INTERACTIONS
national synchrotron light source
PATHOGENS
PROTEINS
SCATTERING
VIRULENCE
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Summary: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 μ-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.
ISSN:0021-9258
1083-351X
DOI:10.1074/jbc.M808954200