6HP7

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

6HP7 の概要

• エントリーDOI: 10.2210/pdb6hp7/pdb
• 分子名称: SPBc2 prophage-derived uncharacterized protein YopK, DNA (43-MER), PHOSPHATE ION, ... (5 entities in total)
• 機能のキーワード: arbitrium peptide receptor, spbeta phage, dna binding protein
• 由来する生物種: Bacillus subtilis (strain 168); 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 117785.86

構造登録者

Marina, A.,Gallego del Sol, F. (登録日: 2018-09-19, 公開日: 2019-02-13, 最終更新日: 2024-05-15)

主引用文献

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

実験手法

X-RAY DIFFRACTION (2.2 Å)