5ZW5

Structure of SeMet-spAimR

5ZW5 の概要

• エントリーDOI: 10.2210/pdb5zw5/pdb
• 分子名称: AimR transcriptional regulator (2 entities in total)
• 機能のキーワード: dimer, spbeta phage, transcription regulator
• 由来する生物種: Bacillus phage SPbeta (Bacillus phage SPBc2)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 91698.95

構造登録者

Cheng, W.,Dou, C. (登録日: 2018-05-14, 公開日: 2018-08-29, 最終更新日: 2024-11-13)

主引用文献

Dou, C.,Xiong, J.,Gu, Y.,Yin, K.,Wang, J.,Hu, Y.,Zhou, D.,Fu, X.,Qi, S.,Zhu, X.,Yao, S.,Xu, H.,Nie, C.,Liang, Z.,Yang, S.,Wei, Y.,Cheng, W.
Structural and functional insights into the regulation of the lysis-lysogeny decision in viral communities.
Nat Microbiol, 3:1285-1294, 2018

PubMed Abstract: Communication is vital for all organisms including microorganisms, which is clearly demonstrated by the bacterial quorum-sensing system. However, the molecular mechanisms underlying communication among viruses (phages) via the quorum-sensing-like 'arbitrium' system remain unclear. Viral or host densities are known to be related to an increased prevalence of lysogeny; however, how the switch from the lytic to the lysogenic pathway occurs is unknown. Thus, we sought to reveal mechanisms of communication among viruses and determine the lysogenic dynamics involved. Structural and functional analyses of the phage-derived SAIRGA and GMPRGA peptides and their corresponding receptors, phAimR and spAimR, indicated that SAIRGA directs the lysis-lysogeny decision of phi3T by modulating conformational changes in phAimR, whereas GMPRGA regulates the lysis-lysogeny pathway by stabilizing spAimR in the dimeric state. Although temperate viruses are thought to share a similar lytic-lysogenic cycle switch model, our study suggests the existence of alternative strain-specific mechanisms that regulate the lysis-lysogeny decision. Collectively, these findings provide insights into the molecular mechanisms underlying communication among viruses, offering theoretical applications for the treatment of infectious viral diseases.

PubMed: 30323253
DOI: 10.1038/s41564-018-0259-7

実験手法

X-RAY DIFFRACTION (2.4 Å)