7P4A

Non-canonical Staphylococcus aureus pathogenicity island repression.

7P4A の概要

• エントリーDOI: 10.2210/pdb7p4a/pdb
• 分子名称: Stl, Sri (3 entities in total)
• 機能のキーワード: mobile genetic element, repressor, sapi, hth domain, dna binding protein
• 由来する生物種: Staphylococcus aureus; 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 72063.79

構造登録者

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. (登録日: 2021-07-10, 公開日: 2022-07-27, 最終更新日: 2024-11-13)

主引用文献

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

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: 36200825
DOI: 10.1093/nar/gkac855

実験手法

X-RAY DIFFRACTION (2.901 Å)