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- W2897903345 abstract "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 aeruginosa, Acinetobacter 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." @default.
- W2897903345 created "2018-10-26" @default.
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- W2897903345 date "2018-12-01" @default.
- W2897903345 modified "2023-10-15" @default.
- W2897903345 title "Crystal structures and biochemical characterization of DNA sliding clamps from three Gram-negative bacterial pathogens" @default.
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- W2897903345 doi "https://doi.org/10.1016/j.jsb.2018.10.008" @default.
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