8BAS

E. coli C7 DarT1 in complex with carba-NAD and DNA

8BAS の概要

• エントリーDOI: 10.2210/pdb8bas/pdb
• 分子名称: E. coli C7 DarT1, DNA (5'-D(*AP*AP*GP*AP*C)-3'), CARBA-NICOTINAMIDE-ADENINE-DINUCLEOTIDE, ... (5 entities in total)
• 機能のキーワード: toxin-antitoxin, dna adp-ribosylation, adp-ribosyltransferase activity, dna binding, toxin
• 由来する生物種: Escherichia coli; 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 26852.16

構造登録者

Schuller, M.,Ariza, A. (登録日: 2022-10-11, 公開日: 2023-07-12, 最終更新日: 2024-02-07)

主引用文献

Schuller, M.,Raggiaschi, R.,Mikolcevic, P.,Rack, J.G.M.,Ariza, A.,Zhang, Y.,Ledermann, R.,Tang, C.,Mikoc, A.,Ahel, I.
Molecular basis for the reversible ADP-ribosylation of guanosine bases.
Mol.Cell, 83:2303-, 2023

PubMed Abstract: Modification of nucleic acids by ADP-ribosylation is catalyzed by various ADP-ribosyltransferases, including the DarT enzyme. The latter is part of the bacterial toxin-antitoxin (TA) system DarTG, which was shown to provide control of DNA replication and bacterial growth as well as protection against bacteriophages. Two subfamilies have been identified, DarTG1 and DarTG2, which are distinguished by their associated antitoxins. While DarTG2 catalyzes reversible ADP-ribosylation of thymidine bases employing a macrodomain as antitoxin, the DNA ADP-ribosylation activity of DarTG1 and the biochemical function of its antitoxin, a NADAR domain, are as yet unknown. Using structural and biochemical approaches, we show that DarT1-NADAR is a TA system for reversible ADP-ribosylation of guanosine bases. DarT1 evolved the ability to link ADP-ribose to the guanine amino group, which is specifically hydrolyzed by NADAR. We show that guanine de-ADP-ribosylation is also conserved among eukaryotic and non-DarT-associated NADAR members, indicating a wide distribution of reversible guanine modifications beyond DarTG systems.

PubMed: 37390817
DOI: 10.1016/j.molcel.2023.06.013

実験手法

X-RAY DIFFRACTION (1.92 Å)