6AMS

Crystal structure of the DNA polymerase III subunit beta from Pseudomonas aeruginosa

Summary for 6AMS

• Entry DOI: 10.2210/pdb6ams/pdb
• Related: 6AMQ 6AP4
• Descriptor: Beta sliding clamp, PHOSPHATE ION (3 entities in total)
• Functional Keywords: dna binding, dna directed dna polymerase activity, transferase
• Biological source: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
• Total number of polymer chains: 4
• Total formula weight: 163337.30

Authors

McGrath, A.E.,Oakley, A.J. (deposition date: 2017-08-11, release date: 2017-11-01, Last modification date: 2023-10-04)

Primary citation

McGrath, A.E.,Martyn, A.P.,Whittell, L.R.,Dawes, F.E.,Beck, J.L.,Dixon, N.E.,Kelso, M.J.,Oakley, A.J.
Crystal structures and biochemical characterization of DNA sliding clamps from three Gram-negative bacterial pathogens.
J. Struct. Biol., 204:396-405, 2018

PubMed 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.

PubMed: 30366028
DOI: 10.1016/j.jsb.2018.10.008

Experimental method

X-RAY DIFFRACTION (2.39 Å)