ArticleThe EMBO journal2000
Crystal structure of a repair enzyme of oxidatively damaged DNA, MutM (Fpg), from an extreme thermophile, Thermus thermophilus HB8.
Article in The EMBO journal, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 56 papers.
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56 citing papers in PubMed, 147 citations in OpenAlex.
- The H2TH-like motif of the Escherichia coli multifunctional protein KsgA is required for DNA binding involved in DNA repair and the suppression of mutation frequencies.Genes and environment : the official journal of the Japanese Environmental Mutagen Society · 2023Article
- Model of abasic site DNA cross-link repair; from the architecture of NEIL3 DNA binding domains to the X-structure model.Nucleic acids research · 2022Article
- Article
- Bacterial DNA excision repair pathways.Nature reviews. Microbiology · 2022Review
- DNA Oxidative Damage as a Sensitive Genetic Endpoint to Detect the Genotoxicity Induced by Titanium Dioxide Nanoparticles.Nanomaterials (Basel, Switzerland) · 2022Article
- Recognition of a tandem lesion by DNA bacterial formamidopyrimidine glycosylases explored combining molecular dynamics and machine learning.Computational and structural biotechnology journal · 2021Article
- Structural Aspects of DNA Repair and Recombination in Crop Improvement.Frontiers in genetics · 2020Review
- DNA Base Excision Repair in Plants: An Unfolding Story With Familiar and Novel Characters.Frontiers in plant science · 2019Review
- Incomplete base excision repair contributes to cell death from antibiotics and other stresses.DNA repair · 2018Review
- Topoisomerase VI senses and exploits both DNA crossings and bends to facilitate strand passage.eLife · 2018Article
- Molecular dynamics simulation of the opposite-base preference and interactions in the active site of formamidopyrimidine-DNA glycosylase.BMC structural biology · 2017Article
- Insights into the glycosylase search for damage from single-molecule fluorescence microscopy.DNA repair · 2014Review
- Repair of oxidative DNA damage and cancer: recent progress in DNA base excision repair.Antioxidants & redox signaling · 2014Review
- A highly conserved family of domains related to the DNA-glycosylase fold helps predict multiple novel pathways for RNA modifications.RNA biology · 2014Article
- DNA glycosylases search for and remove oxidized DNA bases.Environmental and molecular mutagenesis · 2013Review
- A novel nucleoid-associated protein specific to the actinobacteria.Nucleic acids research · 2013Article
- Base excision repair.Cold Spring Harbor perspectives in biology · 2013Review
- Structural characterization of a mouse ortholog of human NEIL3 with a marked preference for single-stranded DNA.Structure (London, England : 1993) · 2013Article
- Recent advances in the structural mechanisms of DNA glycosylases.Biochimica et biophysica acta · 2013Review
- Structural and biochemical studies of a plant formamidopyrimidine-DNA glycosylase reveal why eukaryotic Fpg glycosylases do not excise 8-oxoguanine.DNA repair · 2012Article
Corrections and comments
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Authors and funding
8 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The MutM [formamidopyrimidine DNA glycosylase (Fpg)] protein is a trifunctional DNA base excision repair enzyme that removes a wide range of oxidatively damaged bases (N-glycosylase activity) and cleaves both the 3'- and 5'-phosphodiester bonds of the resulting apurinic/apyrimidinic site (AP lyase activity). The crystal structure of MutM from an extreme thermophile, Thermus thermophilus HB8, was determined at 1.9 A resolution with multiwavelength anomalous diffraction phasing using the intrinsic Zn(2+) ion of the zinc finger. MutM is composed of two distinct and novel domains connected by a flexible hinge. There is a large, electrostatically positive cleft lined by highly conserved residues between the domains. On the basis of the three-dimensional structure and taking account of previous biochemical experiments, we propose a DNA-binding mode and reaction mechanism for MutM. The locations of the putative catalytic residues and the two DNA-binding motifs (the zinc finger and the helix-two-turns-helix motifs) suggest that the oxidized base is flipped out from double-stranded DNA in the binding mode and excised by a catalytic mechanism similar to that of bifunctional base excision repair enzymes.
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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.