6AMQ

Crystal structure of the DNA polymerase III subunit beta from Enterobacter cloacae

6AMQ の概要

• エントリーDOI: 10.2210/pdb6amq/pdb
• 関連するPDBエントリー: 6AMS 6AP4
• 分子名称: DNA polymerase III subunit beta, SULFATE ION (3 entities in total)
• 機能のキーワード: dna binding, dna directed dna polymerase activity, transferase
• 由来する生物種: Enterobacter cloacae EcWSU1
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 162385.10

構造登録者

McGrath, A.E.,Oakley, A.J. (登録日: 2017-08-11, 公開日: 2017-11-01, 最終更新日: 2023-10-04)

主引用文献

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

実験手法

X-RAY DIFFRACTION (2.67 Å)