ArticleThe Journal of biological chemistry2009
Structural characterization of a viral NEIL1 ortholog unliganded and bound to abasic site-containing DNA.
Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.
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Who cites it
30 citing papers in PubMed, 45 citations in OpenAlex.
- Functional characterization of single nucleotide polymorphic variants of DNA repair enzyme NEIL1 in South Asian populations.DNA repair · 2024Article
- Structural and biochemical insights into NEIL2's preference for abasic sites.Nucleic acids research · 2023Article
- Mycobacterial helicase Lhr abets resistance to DNA crosslinking agents mitomycin C and cisplatin.Nucleic acids research · 2023Article
- Article
- A Low-Activity Polymorphic Variant of Human NEIL2 DNA Glycosylase.International journal of molecular sciences · 2022Article
- Recognition and repair of oxidatively generated DNA lesions in plasmid DNA by a facilitated diffusion mechanism.The Biochemical journal · 2021Article
- Formation and processing of DNA damage substrates for the hNEIL enzymes.Free radical biology & medicine · 2017Review
- Tautomerization-dependent recognition and excision of oxidation damage in base-excision DNA repair.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Phosphorylation Sites Identified in the NEIL1 DNA Glycosylase Are Potential Targets for the JNK1 Kinase.PloS one · 2016Article
- Base Excision Repair in the Mitochondria.Journal of cellular biochemistry · 2015Review
- Base excision repair: a critical player in many games.DNA repair · 2014Review
- Two glycosylase families diffusively scan DNA using a wedge residue to probe for and identify oxidatively damaged bases.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Genome and cancer single nucleotide polymorphisms of the human NEIL1 DNA glycosylase: activity, structure, and the effect of editing.DNA repair · 2014Article
- Zinc finger oxidation of Fpg/Nei DNA glycosylases by 2-thioxanthine: biochemical and X-ray structural characterization.Nucleic acids research · 2014Article
- DNA glycosylases search for and remove oxidized DNA bases.Environmental and molecular mutagenesis · 2013Review
- Article
- Non-productive DNA damage binding by DNA glycosylase-like protein Mag2 from Schizosaccharomyces pombe.DNA repair · 2013Article
- Structural characterization of a mouse ortholog of human NEIL3 with a marked preference for single-stranded DNA.Structure (London, England : 1993) · 2013Article
- Sculpting of DNA at abasic sites by DNA glycosylase homolog mag2.Structure (London, England : 1993) · 2013Article
- Recent advances in the structural mechanisms of DNA glycosylases.Biochimica et biophysica acta · 2013Review
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Endonuclease VIII (Nei) is a DNA glycosylase of the base excision repair pathway that recognizes and excises oxidized pyrimidines. We determined the crystal structures of a NEIL1 ortholog from the giant Mimivirus (MvNei1) unliganded and bound to DNA containing tetrahydrofuran (THF), which is the first structure of any Nei with an abasic site analog. The MvNei1 structures exhibit the same overall architecture as other enzymes of the Fpg/Nei family, which consists of two globular domains joined by a linker region. MvNei1 harbors a zincless finger, first described in human NEIL1, rather than the signature zinc finger generally found in the Fpg/Nei family. In contrast to Escherichia coli Nei, where a dramatic conformational change was observed upon binding DNA, the structure of MvNei1 bound to DNA does not reveal any substantial movement compared with the unliganded enzyme. A protein segment encompassing residues 217-245 in MvNei1 corresponds to the "missing loop" in E. coli Nei and the "alphaF-beta10 loop" in E. coli Fpg, which has been reported to be involved in lesion recognition. Interestingly, the corresponding loop in MvNei1 is ordered in both the unliganded and furan-bound structures, unlike other Fpg/Nei enzymes where the loop is generally ordered in the unliganded enzyme or in complexes with a lesion, and disordered otherwise. In the MvNei1.tetrahydrofuran complex a tyrosine located at the tip of the putative lesion recognition loop stacks against the furan ring; the tyrosine is predicted to adopt a different conformation to accommodate a modified base.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.