5M3E

Macrodomain of Thermus aquaticus DarG in complex with ADP-ribose

5M3E の概要

• エントリーDOI: 10.2210/pdb5m3e/pdb
• 分子名称: Appr-1-p processing domain protein, ADENOSINE-5-DIPHOSPHORIBOSE, CHLORIDE ION, ... (4 entities in total)
• 機能のキーワード: macrodomain, adp-ribosylation, adp-ribose, antitoxin, toxin-antitoxin
• 由来する生物種: Thermus aquaticus Y51MC23
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 19379.44

構造登録者

Ariza, A. (登録日: 2016-10-14, 公開日: 2016-12-21, 最終更新日: 2024-01-17)

主引用文献

Jankevicius, G.,Ariza, A.,Ahel, M.,Ahel, I.
The Toxin-Antitoxin System DarTG Catalyzes Reversible ADP-Ribosylation of DNA.
Mol. Cell, 64:1109-1116, 2016

PubMed Abstract: The discovery and study of toxin-antitoxin (TA) systems helps us advance our understanding of the strategies prokaryotes employ to regulate cellular processes related to the general stress response, such as defense against phages, growth control, biofilm formation, persistence, and programmed cell death. Here we identify and characterize a TA system found in various bacteria, including the global pathogen Mycobacterium tuberculosis. The toxin of the system (DarT) is a domain of unknown function (DUF) 4433, and the antitoxin (DarG) a macrodomain protein. We demonstrate that DarT is an enzyme that specifically modifies thymidines on single-stranded DNA in a sequence-specific manner by a nucleotide-type modification called ADP-ribosylation. We also show that this modification can be removed by DarG. Our results provide an example of reversible DNA ADP-ribosylation, and we anticipate potential therapeutic benefits by targeting this enzyme-enzyme TA system in bacterial pathogens such as M. tuberculosis.

PubMed: 27939941
DOI: 10.1016/j.molcel.2016.11.014

実験手法

X-RAY DIFFRACTION (2.5 Å)