期刊
PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS
卷 62, 期 2, 页码 421-434出版社
WILEY
DOI: 10.1002/prot.20767
关键词
cytolethal distending toxin; genotoxin; nuclease; protein-protein interaction; homology modeling
资金
- NIAID NIH HHS [1U19AI056510] Funding Source: Medline
Cytolethal distending toxins (CDTs) constitute a family of bacterial proteins that enter eukaryotic cells with genotoxic activity leading to cell cycle arrest and apoptosis. CDTs are widespread, having been found in a variety of Gramnegative pathogens with a broad tissue tropism. The recently determined crystal structure of the Haemophilus ducreyi CDT provides a powerful starting point for analysis of the structure and function in this toxin family. In this study, we apply comparative modeling and structural analysis to extend the experimental structural information to multiple CDT toxins from a diverse species. Analysis of structurally and functionally important residues in the active subunit, CdtB, and putative cell delivery elements, CdtA and CdtC, begins to establish the fundamental, mechanistic elements of this unique holotoxin. The results reveal that key structural features with important functional consequences are highly conserved across different CDTs, providing a blueprint for directed examination of functional hypotheses in a variety of pathogenic contexts.
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