6L8F

Crystal structure of heterotetrameric complex of YoeB-YefM toxin-antitoxin from Staphylococcus aureus.

6L8F の概要

• エントリーDOI: 10.2210/pdb6l8f/pdb
• 分子名称: YoeB, Antitoxin (3 entities in total)
• 機能のキーワード: toxin-antitoxin, microbial rnase, yoeb, staphylococcus aureus, toxin, toxin-antitoxin complex, toxin/antitoxin
• 由来する生物種: Staphylococcus aureus (strain NCTC 8325); 詳細
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 82917.80

構造登録者

Yue, J.,Xue, L. (登録日: 2019-11-06, 公開日: 2020-09-02, 最終更新日: 2023-11-22)

主引用文献

Xue, L.,Yue, J.,Ke, J.,Khan, M.H.,Wen, W.,Sun, B.,Zhu, Z.,Niu, L.
Distinct oligomeric structures of the YoeB-YefM complex provide insights into the conditional cooperativity of type II toxin-antitoxin system.
Nucleic Acids Res., 48:10527-10541, 2020

PubMed Abstract: YoeB-YefM, the widespread type II toxin-antitoxin (TA) module, binds to its own promoter to autoregulate its transcription: repress or induce transcription under normal or stress conditions, respectively. It remains unclear how YoeB-YefM regulates its transcription depending on the YoeB to YefM TA ratio. We find that YoeB-YefM complex from S.aureus exists as two distinct oligomeric assemblies: heterotetramer (YoeB-YefM2-YoeB) and heterohexamer (YoeB-YefM2-YefM2-YoeB) with low and high DNA-binding affinities, respectively. Structures of the heterotetramer alone and heterohexamer bound to promoter DNA reveals that YefM C-terminal domain undergoes disorder to order transition upon YoeB binding, which allosterically affects the conformation of N-terminal DNA-binding domain. At TA ratio of 1:2, unsaturated binding of YoeB to the C-terminal regions of YefM dimer forms an optimal heterohexamer for DNA binding, and two YefM dimers with N-terminal domains dock into the adjacent major grooves of DNA to specifically recognize the 5'-TTGTACAN6AGTACAA-3' palindromic sequence, resulting in transcriptional repression. In contrast, at TA ratio of 1:1, binding of two additional YoeB molecules onto the heterohexamer induces the completely ordered conformation of YefM and disassembles the heterohexamer into two heterotetramers, which are unable to bind the promoter DNA optimally due to steric clashes, hence derepresses TA operon transcription.

PubMed: 32845304
DOI: 10.1093/nar/gkaa706

実験手法

X-RAY DIFFRACTION (2.4 Å)