6N90

YoeB/ParE toxin from Agrobacterium tumefaciens

6N90 の概要

• エントリーDOI: 10.2210/pdb6n90/pdb
• 分子名称: Uncharacterized protein, 6-tungstotellurate(VI) (3 entities in total)
• 機能のキーワード: toxin
• 由来する生物種: Agrobacterium tumefaciens
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 24332.56

構造登録者

Bourne, C.R.,Reddem, E.R. (登録日: 2018-11-30, 公開日: 2019-11-06, 最終更新日: 2023-10-11)

主引用文献

Ames, J.R.,McGillick, J.,Murphy, T.,Reddem, E.,Bourne, C.R.
Identifying a Molecular Mechanism That Imparts Species-Specific Toxicity to YoeB Toxins.
Front Microbiol, 11:959-959, 2020

PubMed Abstract: The ribosome-dependent (Ec) mRNase toxin YoeB has been demonstrated to protect cells during thermal stress. (At), a plant pathogen, also encodes a YoeB toxin. Initial studies indicated that AtYoeB does not impact the growth of Ec, but its expression is toxic to the native host At. The current work examines this species-specific effect. We establish the highly similar structure and function of Ec and AtYoeB toxins, including the ability of the AtYoeB toxin to inhibit Ec ribosomes . Comparison of YoeB sequences and structures highlights a four-residue helix between β-strands 2 and 3 that interacts with mRNA bases within the ribosome. This helix sequence is varied among YoeB toxins, and this variation correlates with bacterial classes of proteobacteria. When the four amino acid sequence of this helix is transplanted from EcYoeB onto AtYoeB, the resulting chimera gains toxicity to Ec cells and lessens toxicity to At cells. The reverse is also true, such that EcYoeB with the AtYoeB helix sequence is less toxic to Ec and gains toxicity to At cultures. We suggest this helix sequence directs mRNA sequence-specific degradation, which varies among proteobacterial classes, and thus controls growth inhibition and YoeB toxicity.

PubMed: 32528435
DOI: 10.3389/fmicb.2020.00959

実験手法

X-RAY DIFFRACTION (1.755 Å)