5MIL

Pirating conserved phage mechanisms promotes promiscuous staphylococcal pathogenicity islands transfer.

5MIL の概要

• エントリーDOI: 10.2210/pdb5mil/pdb
• 分子名称: DUTPase family protein, 2'-DEOXYURIDINE 5'-ALPHA,BETA-IMIDO-TRIPHOSPHATE, MAGNESIUM ION, ... (4 entities in total)
• 機能のキーワード: dutpase, dimeric dutpase, deoxyuridine triphosphatase, hydrolase
• 由来する生物種: Staphylococcus aureus
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 46821.58

構造登録者

Donderis, J.,Marina, A.,Penades, J.R. (登録日: 2016-11-28, 公開日: 2017-09-06, 最終更新日: 2024-05-08)

主引用文献

Bowring, J.,Neamah, M.M.,Donderis, J.,Mir-Sanchis, I.,Alite, C.,Ciges-Tomas, J.R.,Maiques, E.,Medmedov, I.,Marina, A.,Penades, J.R.
Pirating conserved phage mechanisms promotes promiscuous staphylococcal pathogenicity island transfer.
Elife, 6:-, 2017

PubMed Abstract: Targeting conserved and essential processes is a successful strategy to combat enemies. Remarkably, the clinically important pathogenicity islands (SaPIs) use this tactic to spread in nature. SaPIs reside passively in the host chromosome, under the control of the SaPI-encoded master repressor, Stl. It has been assumed that SaPI de-repression is effected by specific phage proteins that bind to Stl, initiating the SaPI cycle. Different SaPIs encode different Stl repressors, so each targets a specific phage protein for its de-repression. Broadening this narrow vision, we report here that SaPIs ensure their promiscuous transfer by targeting conserved phage mechanisms. This is accomplished because the SaPI Stl repressors have acquired different domains to interact with unrelated proteins, encoded by different phages, but in all cases performing the same conserved function. This elegant strategy allows intra- and inter-generic SaPI transfer, highlighting these elements as one of nature's most fascinating subcellular parasites.

PubMed: 28826473
DOI: 10.7554/eLife.26487

実験手法

X-RAY DIFFRACTION (2.1 Å)