6YSE

Gp4 from the Pseudomonas phage LUZ24

Summary for 6YSE

• Entry DOI: 10.2210/pdb6yse/pdb
• NMR Information: BMRB: 28112
• Descriptor: Gp4 (1 entity in total)
• Functional Keywords: gp4, phage, antimicrobial, pseudomonas, peptide binding protein
• Biological source: Pseudomonas phage LUZ24
• Total number of polymer chains: 1
• Total formula weight: 5668.79

Authors

Bdira, F.B.,Volkov, A.N.,Dame, R.T. (deposition date: 2020-04-22, release date: 2021-05-12, Last modification date: 2024-06-19)

Primary citation

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

Experimental method

SOLUTION NMR