6S7I
Arbitrium receptor from a Bacillus subtilis Katmira33 phage
Summary for 6S7I
| Entry DOI | 10.2210/pdb6s7i/pdb |
| Descriptor | Arbitrium receptor, SULFATE ION (3 entities in total) |
| Functional Keywords | arbitrium, dna binding protein |
| Biological source | Bacillus subtilis |
| Total number of polymer chains | 2 |
| Total formula weight | 91049.96 |
| Authors | Marina, A.,Gallego del Sol, F. (deposition date: 2019-07-05, release date: 2021-04-14, Last modification date: 2024-01-24) |
| Primary citation | Gallego Del Sol, F.,Quiles-Puchalt, N.,Brady, A.,Penades, J.R.,Marina, A. Insights into the mechanism of action of the arbitrium communication system in SPbeta phages. Nat Commun, 13:3627-3627, 2022 Cited by PubMed Abstract: The arbitrium system is employed by phages of the SPbeta family to communicate with their progeny during infection to decide either to follow the lytic or the lysogenic cycle. The system is controlled by a peptide, AimP, that binds to the regulator AimR, inhibiting its DNA-binding activity and expression of aimX. Although the structure of AimR has been elucidated for phages SPβ and phi3T, there is still controversy regarding the molecular mechanism of AimR function, with two different proposed models for SPβ. In this study, we deepen our understanding of the system by solving the structure of an additional AimR that shows chimerical characteristics with the SPβ receptor. The crystal structures of this AimR (apo, AimP-bound and DNA-bound) together with in vitro and in vivo analyses confirm a mechanism of action by AimP-induced conformational restriction, shedding light on peptide specificity and cross regulation with relevant biological implications. PubMed: 35750663DOI: 10.1038/s41467-022-31144-3 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.4 Å) |
Structure validation
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