6YSE

Gp4 from the Pseudomonas phage LUZ24

6YSE の概要

• エントリーDOI: 10.2210/pdb6yse/pdb
• NMR情報: BMRB: 28112
• 分子名称: Gp4 (1 entity in total)
• 機能のキーワード: gp4, phage, antimicrobial, pseudomonas, peptide binding protein
• 由来する生物種: Pseudomonas phage LUZ24
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 5668.79

構造登録者

Bdira, F.B.,Volkov, A.N.,Dame, R.T. (登録日: 2020-04-22, 公開日: 2021-05-12, 最終更新日: 2024-06-19)

主引用文献

Bdira, F.B.,Erkelens, A.M.,Qin, L.,Volkov, A.N.,Lippa, A.M.,Bowring, N.,Boyle, A.L.,Ubbink, M.,Dove, S.L.,Dame, R.T.
Novel anti-repression mechanism of H-NS proteins by a phage protein.
Nucleic Acids Res., 49:10770-10784, 2021

PubMed Abstract: H-NS family proteins, bacterial xenogeneic silencers, play central roles in genome organization and in the regulation of foreign genes. It is thought that gene repression is directly dependent on the DNA binding modes of H-NS family proteins. These proteins form lateral protofilaments along DNA. Under specific environmental conditions they switch to bridging two DNA duplexes. This switching is a direct effect of environmental conditions on electrostatic interactions between the oppositely charged DNA binding and N-terminal domains of H-NS proteins. The Pseudomonas lytic phage LUZ24 encodes the protein gp4, which modulates the DNA binding and function of the H-NS family protein MvaT of Pseudomonas aeruginosa. However, the mechanism by which gp4 affects MvaT activity remains elusive. In this study, we show that gp4 specifically interferes with the formation and stability of the bridged MvaT-DNA complex. Structural investigations suggest that gp4 acts as an 'electrostatic zipper' between the oppositely charged domains of MvaT protomers, and stabilizes a structure resembling their 'half-open' conformation, resulting in relief of gene silencing and adverse effects on P. aeruginosa growth. The ability to control H-NS conformation and thereby its impact on global gene regulation and growth might open new avenues to fight Pseudomonas multidrug resistance.

PubMed: 34520554
DOI: 10.1093/nar/gkab793

実験手法

SOLUTION NMR