Flexible structural arrangement and DNA-binding properties of protein p6 from Bacillus subtillis phage φ29.

ABSTRACT: The genome-organizing protein p6 of Bacillus subtilis bacteriophage φ29 plays an essential role in viral development by activating the initiation of DNA replication and participating in the early-to-late transcriptional switch. These activities require the formation of a nucleoprotein complex in which the DNA adopts a right-handed superhelix wrapping around a multimeric p6 scaffold, restraining positive supercoiling and compacting the viral genome. Due to the absence of homologous structures, prior attempts to unveil p6's structural architecture failed. Here, we employed AlphaFold2 to engineer rational p6 constructs yielding crystals for three-dimensional structure determination. Our findings reveal a novel fold adopted by p6 that sheds light on its self-association mechanism and its inter

SUBMITTER: Alcorlo M 

PROVIDER: S-EPMC10899789 | biostudies-literature | 2024 Feb

REPOSITORIES: biostudies-literature