7ZVI
Non-canonical Staphylococcus aureus pathogenicity island repression
Summary for 7ZVI
Entry DOI | 10.2210/pdb7zvi/pdb |
Descriptor | Orf22, Sri (3 entities in total) |
Functional Keywords | mobile genetic element, repressor, sapi, hth domain, dna binding protein, gene regulation |
Biological source | Staphylococcus aureus More |
Total number of polymer chains | 2 |
Total formula weight | 36191.12 |
Authors | Miguel-Romero, L.,Alqasmi, M.,Bacarizo, J.,Marina, A.,Penades, J.R. (deposition date: 2022-05-16, release date: 2022-09-28, Last modification date: 2024-01-31) |
Primary citation | Miguel-Romero, L.,Alqasmi, M.,Bacarizo, J.,Tan, J.A.,Cogdell, R.J.,Chen, J.,Byron, O.,Christie, G.E.,Marina, A.,Penades, J.R. Non-canonical Staphylococcus aureus pathogenicity island repression. Nucleic Acids Res., 50:11109-11127, 2022 Cited by PubMed Abstract: Mobile genetic elements control their life cycles by the expression of a master repressor, whose function must be disabled to allow the spread of these elements in nature. Here, we describe an unprecedented repression-derepression mechanism involved in the transfer of Staphylococcus aureus pathogenicity islands (SaPIs). Contrary to the classical phage and SaPI repressors, which are dimers, the SaPI1 repressor StlSaPI1 presents a unique tetrameric conformation never seen before. Importantly, not just one but two tetramers are required for SaPI1 repression, which increases the novelty of the system. To derepress SaPI1, the phage-encoded protein Sri binds to and induces a conformational change in the DNA binding domains of StlSaPI1, preventing the binding of the repressor to its cognate StlSaPI1 sites. Finally, our findings demonstrate that this system is not exclusive to SaPI1 but widespread in nature. Overall, our results characterize a novel repression-induction system involved in the transfer of MGE-encoded virulence factors in nature. PubMed: 36200825DOI: 10.1093/nar/gkac855 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.973 Å) |
Structure validation
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