6LW3

Crystal structure of RuvC from Pseudomonas aeruginosa

6LW3 の概要

• エントリーDOI: 10.2210/pdb6lw3/pdb
• 分子名称: Crossover junction endodeoxyribonuclease RuvC (2 entities in total)
• 機能のキーワード: holliday junction; resolvase; ruvc; endonuclease, dna binding protein
• 由来する生物種: Pseudomonas aeruginosa
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 34499.98

構造登録者

Hu, Y.,He, Y.,Lin, Z. (登録日: 2020-02-07, 公開日: 2020-02-26, 最終更新日: 2023-11-29)

主引用文献

Hu, Y.,He, Y.,Lin, Z.
Biochemical and structural characterization of the Holliday junction resolvase RuvC from Pseudomonas aeruginosa.
Biochem.Biophys.Res.Commun., 525:265-271, 2020

PubMed Abstract: The Holliday junction, a four-way DNA structure, is an important intermediate of homologous recombination. Proper Holliday junction resolution is critical to complete the recombination process. In most bacterial cells, the Holliday junction cleavage is mainly performed by a specific endonuclease RuvC. Here, we describe the biochemical properties and the crystal structure of RuvC from an opportunistic pathogen, Pseudomonas aeruginosa (PaRuvC). PaRuvC specifically binds to the Holliday junction DNA and preferentially cleaves it at the consensus 5'-TTC-3'. PaRuvC uses Mg as the preferred divalent metal cofactor for Holliday junction cleavage and its optimum pH is 8.0-9.0. Elevated temperatures (37-60 °C) boost the catalytic activity, but temperatures higher than 53 °C reduce the protein stability. The crystal structure of PaRuvC determined at 2.4 Å and mutagenesis analysis reveal key residues involved in the dimer formation, substrate binding and catalysis. Our results are expected to provide useful information to combat antibiotic resistance of Pseudomonas aeruginosa by targeting its homologous recombination system.

PubMed: 32085896
DOI: 10.1016/j.bbrc.2020.02.062

実験手法

X-RAY DIFFRACTION (2.38 Å)