6HP7

ARBITRIUM PEPTIDE RECEPTOR FROM SPBETA PHAGE in complex with 43 mer DNA

Summary for 6HP7

• Entry DOI: 10.2210/pdb6hp7/pdb
• Descriptor: SPBc2 prophage-derived uncharacterized protein YopK, DNA (43-MER), PHOSPHATE ION, ... (5 entities in total)
• Functional Keywords: arbitrium peptide receptor, spbeta phage, dna binding protein
• Biological source: Bacillus subtilis (strain 168); More
• Total number of polymer chains: 4
• Total formula weight: 117785.86

Authors

Marina, A.,Gallego del Sol, F. (deposition date: 2018-09-19, release date: 2019-02-13, Last modification date: 2024-05-15)

Primary citation

Gallego Del Sol, F.,Penades, J.R.,Marina, A.
Deciphering the Molecular Mechanism Underpinning Phage Arbitrium Communication Systems.
Mol.Cell, 74:59-72.e3, 2019

PubMed Abstract: Bacillus phages use a communication system, termed "arbitrium," to coordinate lysis-lysogeny decisions. Arbitrium communication is mediated by the production and secretion of a hexapeptide (AimP) during lytic cycle. Once internalized, AimP reduces the expression of the negative regulator of lysogeny, AimX, by binding to the transcription factor, AimR, promoting lysogeny. We have elucidated the crystal structures of AimR from the Bacillus subtilis SPbeta phage in its apo form, bound to its DNA operator and in complex with AimP. AimR presents intrinsic plasticity, sharing structural features with the RRNPP quorum-sensing family. Remarkably, AimR binds to an unusual operator with a long spacer that interacts nonspecifically with the receptor TPR domain, while the HTH domain canonically recognizes two inverted repeats. AimP stabilizes a compact conformation of AimR that approximates the DNA-recognition helices, preventing AimR binding to the aimX promoter region. Our results establish the molecular basis of the arbitrium communication system.

PubMed: 30745087
DOI: 10.1016/j.molcel.2019.01.025

Experimental method

X-RAY DIFFRACTION (2.2 Å)