5M3E
Macrodomain of Thermus aquaticus DarG in complex with ADP-ribose
Summary for 5M3E
| Entry DOI | 10.2210/pdb5m3e/pdb |
| Descriptor | Appr-1-p processing domain protein, ADENOSINE-5-DIPHOSPHORIBOSE, CHLORIDE ION, ... (4 entities in total) |
| Functional Keywords | macrodomain, adp-ribosylation, adp-ribose, antitoxin, toxin-antitoxin |
| Biological source | Thermus aquaticus Y51MC23 |
| Total number of polymer chains | 1 |
| Total formula weight | 19379.44 |
| Authors | Ariza, A. (deposition date: 2016-10-14, release date: 2016-12-21, Last modification date: 2024-01-17) |
| Primary citation | 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 Cited by 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: 27939941DOI: 10.1016/j.molcel.2016.11.014 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.5 Å) |
Structure validation
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