ArticleProceedings of the National Academy of Sciences of the United States of America2009
Mechanism of ADP-ribosylation removal revealed by the structure and ligand complexes of the dimanganese mono-ADP-ribosylhydrolase DraG.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed, 35 citations in OpenAlex.
- Insights into mechanisms of ubiquitin ADP-ribosylation reversal.Biochemical Society transactions · 2024Review
- Genome features of a novel hydrocarbonoclastic Chryseobacterium oranimense strain and its comparison to bacterial oil-degraders and to other C. oranimense strains.DNA research : an international journal for rapid publication of reports on genes and genomes · 2023Article
- The DarT/DarG Toxin-Antitoxin ADP-Ribosylation System as a Novel Target for a Rational Design of Innovative Antimicrobial Strategies.Pathogens (Basel, Switzerland) · 2023Article
- Newly identified HMO-2011-type phages reveal genomic diversity and biogeographic distributions of this marine viral group.The ISME journal · 2022Article
- ADP-ribosylation systems in bacteria and viruses.Computational and structural biotechnology journal · 2021Review
- Snapshots of ADP-ribose bound to Getah virus macro domain reveal an intriguing choreography.Scientific reports · 2020Article
- (ADP-ribosyl)hydrolases: structure, function, and biology.Genes & development · 2020Review
- Targeting ADP-ribosylation as an antimicrobial strategy.Biochemical pharmacology · 2019Review
- ADP-ribosylation signalling and human disease.Open biology · 2019Review
- (ADP-ribosyl)hydrolases: Structural Basis for Differential Substrate Recognition and Inhibition.Cell chemical biology · 2018Article
- Bifunctional Immunity Proteins Protect Bacteria against FtsZ-Targeting ADP-Ribosylating Toxins.Cell · 2018Article
- Structure-function analyses reveal the mechanism of the ARH3-dependent hydrolysis of ADP-ribosylation.The Journal of biological chemistry · 2018Article
- Structure of human ADP-ribosyl-acceptor hydrolase 3 bound to ADP-ribose reveals a conformational switch that enables specific substrate recognition.The Journal of biological chemistry · 2018Article
- Energy shifts induce membrane sequestration of DraG in Rhodospirillum rubrum independent of the ammonium transporters and diazotrophic conditions.FEMS microbiology letters · 2018Article
- ADP-ribosylation: new facets of an ancient modification.The FEBS journal · 2017Review
- The cardiac-restricted protein ADP-ribosylhydrolase-like 1 is essential for heart chamber outgrowth and acts on muscle actin filament assembly.Developmental biology · 2016Article
- Influence of different factors on the nitrogenase activity of the engineered Escherichia coli 78-7.World journal of microbiology & biotechnology · 2015Article
- Assembly of nonheme Mn/Fe active sites in heterodinuclear metalloproteins.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2014Review
- Post-translational modification of P II signal transduction proteins.Frontiers in microbiology · 2014Review
- Structural biology of the writers, readers, and erasers in mono- and poly(ADP-ribose) mediated signaling.Molecular aspects of medicine · 2013Review
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
ADP-ribosylation is a ubiquitous regulatory posttranslational modification involved in numerous key processes such as DNA repair, transcription, cell differentiation, apoptosis, and the pathogenic mechanism of certain bacterial toxins. Despite the importance of this reversible process, very little is known about the structure and mechanism of the hydrolases that catalyze removal of the ADP-ribose moiety. In the phototrophic bacterium Rhodospirillum rubrum, dinitrogenase reductase-activating glycohydrolase (DraG), a dimanganese enzyme that reversibly associates with the cell membrane, is a key player in the regulation of nitrogenase activity. DraG has long served as a model protein for ADP-ribosylhydrolases. Here, we present the crystal structure of DraG in the holo and ADP-ribose bound forms. We also present the structure of a reaction intermediate analogue and propose a detailed catalytic mechanism for protein de-ADP-ribosylation involving ring opening of the substrate ribose. In addition, the particular manganese coordination in DraG suggests a rationale for the enzyme's preference for manganese over magnesium, although not requiring a redox active metal for the reaction.
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