Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

8BJV

Crystal structure of YopR

Summary for 8BJV
Entry DOI10.2210/pdb8bjv/pdb
Related8B6J
DescriptorSPbeta prophage-derived uncharacterized protein YopR, GLYCEROL (3 entities in total)
Functional Keywordsyopr, phage-repressor, recombinase, dna binding protein
Biological sourceBacillus subtilis subsp. subtilis str. 168
Total number of polymer chains3
Total formula weight113175.33
Authors
Gallego del Sol, F.,Marina, A. (deposition date: 2022-11-08, release date: 2023-11-22, Last modification date: 2024-05-29)
Primary citationBrady, A.,Cabello-Yeves, E.,Gallego Del Sol, F.,Chmielowska, C.,Mancheno-Bonillo, J.,Zamora-Caballero, S.,Omer, S.B.,Torres-Puente, M.,Eldar, A.,Quiles-Puchalt, N.,Marina, A.,Penades, J.R.
Characterization of a unique repression system present in arbitrium phages of the SPbeta family.
Cell Host Microbe, 31:2023-2037.e8, 2023
Cited by
PubMed Abstract: Arbitrium-coding phages use peptides to communicate and coordinate the decision between lysis and lysogeny. However, the mechanism by which these phages establish lysogeny remains unknown. Here, focusing on the SPbeta phage family's model phages phi3T and SPβ, we report that a six-gene operon called the "SPbeta phages repressor operon" (sro) expresses not one but two master repressors, SroE and SroF, the latter of which folds like a classical phage integrase. To promote lysogeny, these repressors bind to multiple sites in the phage genome. SroD serves as an auxiliary repressor that, with SroEF, forms the repression module necessary for lysogeny establishment and maintenance. Additionally, the proteins SroABC within the operon are proposed to constitute the transducer module, connecting the arbitrium communication system to the activity of the repression module. Overall, this research sheds light on the intricate and specialized repression system employed by arbitrium SPβ-like phages in making lysis-lysogeny decisions.
PubMed: 38035880
DOI: 10.1016/j.chom.2023.11.003
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.2 Å)
Structure validation

246905

PDB entries from 2025-12-31

PDB statisticsPDBj update infoContact PDBjnumon