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5Y24

Crystal structure of AimR from Bacillus phage SPbeta in complex with its signalling peptide

5Y24 の概要
エントリーDOI10.2210/pdb5y24/pdb
分子名称AimR transcriptional regulator, GLY-MET-PRO-ARG-GLY-ALA, BROMIDE ION, ... (4 entities in total)
機能のキーワードdna binding protein, peptide binding protein, complex with peptide
由来する生物種Bacillus phage SPbeta (Bacillus phage SPBc2)
詳細
タンパク質・核酸の鎖数4
化学式量合計96424.53
構造登録者
Wang, Q.,Guan, Z.Y.,Zou, T.T.,Yin, P. (登録日: 2017-07-24, 公開日: 2018-09-19, 最終更新日: 2018-11-28)
主引用文献Wang, Q.,Guan, Z.,Pei, K.,Wang, J.,Liu, Z.,Yin, P.,Peng, D.,Zou, T.
Structural basis of the arbitrium peptide-AimR communication system in the phage lysis-lysogeny decision.
Nat Microbiol, 3:1266-1273, 2018
Cited by
PubMed Abstract: A bacteriophage can replicate and release virions from a host cell in the lytic cycle or switch to a lysogenic process in which the phage integrates itself into the host genome as a prophage. In Bacillus cells, some types of phages employ the arbitrium communication system, which contains an arbitrium hexapeptide, the cellular receptor AimR and the lysogenic negative regulator AimX. This system controls the decision between the lytic and lysogenic cycles. However, both the mechanism of molecular recognition between the arbitrium peptide and AimR and how downstream gene expression is regulated remain unknown. Here, we report crystal structures for AimR from the SPbeta phage in the apo form and the arbitrium peptide-bound form at 2.20 Å and 1.92 Å, respectively. With or without the peptide, AimR dimerizes through the C-terminal capping helix. AimR assembles a superhelical fold and accommodates the peptide encircled by its tetratricopeptide repeats, which is reminiscent of RRNPP family members from the quorum-sensing system. In the absence of the arbitrium peptide, AimR targets the upstream sequence of the aimX gene; its DNA binding activity is prevented following peptide binding. In summary, our findings provide a structural basis for peptide recognition in the phage lysis-lysogeny decision communication system.
PubMed: 30224798
DOI: 10.1038/s41564-018-0239-y
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (1.922 Å)
構造検証レポート
Validation report summary of 5y24
検証レポート(詳細版)ダウンロードをダウンロード

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件を2024-10-30に公開中

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