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Journal of Structural Biology
Volume 204 (3), 2018, Pages 396-405

Crystal structures and biochemical characterization of DNA sliding clamps from three Gram-negative bacterial pathogens

Amy E.Mc Grath, Alexander P.Martyn, Louise R.Whittell, Fay E.Dawes, Jennifer L.Beck, Nicholas E.Dixon, Michael J.Kelso, Aaron J.Oakley

Molecular Horizons and School of Chemistry and Molecular Bioscience, University of Wollongong, and Illawarra Health and Medical Research Institute, Wollongong, New South Wales, Australia.


Bacterial sliding clamps bind to DNA and act as protein-protein interaction hubs for several proteins involved in DNA replication and repair. The partner proteins all bind to a common pocket on sliding clamps via conserved linear peptide sequence motifs, which suggest the pocket as an attractive target for development of new antibiotics. Herein we report the X-ray crystal structures and biochemical characterization of β sliding clamps from the Gram-negative pathogens Pseudomonas aeruginosaAcinetobacter baumannii and Enterobacter cloacae. The structures reveal close similarity between the pathogen and Escherichia coli clamps and similar patterns of binding to linear clamp-binding motif peptides. The results suggest that linear motif-sliding clamp interactions are well conserved and an antibiotic targeting the sliding clamp should have broad-spectrum activity against Gram-negative pathogens.

Graphical abstract

Keywords: Antimicrobials, ESKAPE pathogens, Sliding clamp.

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