8BJV
Crystal structure of YopR
Summary for 8BJV
| Entry DOI | 10.2210/pdb8bjv/pdb |
| Related | 8B6J |
| Descriptor | SPbeta prophage-derived uncharacterized protein YopR, GLYCEROL (3 entities in total) |
| Functional Keywords | yopr, phage-repressor, recombinase, dna binding protein |
| Biological source | Bacillus subtilis subsp. subtilis str. 168 |
| Total number of polymer chains | 3 |
| Total formula weight | 113175.33 |
| Authors | Gallego del Sol, F.,Marina, A. (deposition date: 2022-11-08, release date: 2023-11-22, Last modification date: 2024-05-29) |
| Primary citation | Brady, 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: 38035880DOI: 10.1016/j.chom.2023.11.003 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.2 Å) |
Structure validation
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