ArticleJournal of the American Chemical Society2016
A Catalytic Role for C-H/π Interactions in Base Excision Repair by Bacillus cereus DNA Glycosylase AlkD.
Article in Journal of the American Chemical Society, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 28 citations in OpenAlex.
- AlkD's Conformational Dynamics Regulated by Protein-DNA Interactions for Effective Target Recognition.The journal of physical chemistry letters · 2025Article
- Bacterial DNA excision repair pathways.Nature reviews. Microbiology · 2022Review
- Article
- Base excision repair system targeting DNA adducts of trioxacarcin/LL-D49194 antibiotics for self-resistance.Nucleic acids research · 2022Article
- Structural evolution of a DNA repair self-resistance mechanism targeting genotoxic secondary metabolites.Nature communications · 2021Article
- Non-flipping DNA glycosylase AlkD scans DNA without formation of a stable interrogation complex.Communications biology · 2021Article
- Dissecting C-H∙∙∙π and N-H∙∙∙π Interactions in Two Proteins Using a Combined Experimental and Computational Approach.Scientific reports · 2019Article
- Emerging Roles of DNA Glycosylases and the Base Excision Repair Pathway.Trends in biochemical sciences · 2019Review
- The abundant DNA adductThe Journal of biological chemistry · 2019Article
- Insights into conformational changes in AlkD bound to DNA with a yatakemycin adduct from computational simulations.Theoretical chemistry accounts · 2018Article
- Selective base excision repair of DNA damage by the non-base-flipping DNA glycosylase AlkC.The EMBO journal · 2018Article
- Toxicity and repair of DNA adducts produced by the natural product yatakemycin.Nature chemical biology · 2017Article
- Engineering protein stability with atomic precision in a monomeric miniprotein.Nature chemical biology · 2017Article
- Structure of a DNA glycosylase that unhooks interstrand cross-links.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- A role for the base excision repair enzyme NEIL3 in replication-dependent repair of interstrand DNA cross-links derived from psoralen and abasic sites.DNA repair · 2017Review
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
DNA glycosylases protect genomic integrity by locating and excising aberrant nucleobases. Substrate recognition and excision usually take place in an extrahelical conformation, which is often stabilized by π-stacking interactions between the lesion nucleobase and aromatic side chains in the glycosylase active site. Bacillus cereus AlkD is the only DNA glycosylase known to catalyze base excision without extruding the damaged nucleotide from the DNA helix. Instead of contacting the nucleobase itself, the AlkD active site interacts with the lesion deoxyribose through a series of C-H/π interactions. These interactions are ubiquitous in protein structures, but evidence for their catalytic significance in enzymology is lacking. Here, we show that the C-H/π interactions between AlkD and the lesion deoxyribose participate in catalysis of glycosidic bond cleavage. This is the first demonstration of a catalytic role for C-H/π interactions as intermolecular forces important to DNA repair.
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Registered trials
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