ArticleThe Journal of biological chemistry2010
Entrapment and structure of an extrahelical guanine attempting to enter the active site of a bacterial DNA glycosylase, MutM.
Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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Who cites it
26 citing papers in PubMed.
- Insights into the A-C Mismatch Conformational Ensemble in Duplex DNA and its Role in Genetic Processes through a Structure-based Review.Journal of molecular biology · 2024Review
- Recognition of a tandem lesion by DNA bacterial formamidopyrimidine glycosylases explored combining molecular dynamics and machine learning.Computational and structural biotechnology journal · 2021Article
- Base-flipping dynamics from an intrahelical to an extrahelical state exerted by thymine DNA glycosylase during DNA repair process.Nucleic acids research · 2018Article
- Uncovering universal rules governing the selectivity of the archetypal DNA glycosylase TDG.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Molecular dynamics simulation of the opposite-base preference and interactions in the active site of formamidopyrimidine-DNA glycosylase.BMC structural biology · 2017Article
- A dynamic checkpoint in oxidative lesion discrimination by formamidopyrimidine-DNA glycosylase.Nucleic acids research · 2016Article
- Active destabilization of base pairs by a DNA glycosylase wedge initiates damage recognition.Nucleic acids research · 2015Article
- Insights into the glycosylase search for damage from single-molecule fluorescence microscopy.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
- DNA glycosylases search for and remove oxidized DNA bases.Environmental and molecular mutagenesis · 2013Review
- Early steps of active DNA demethylation initiated by ROS1 glycosylase require three putative helix-invading residues.Nucleic acids research · 2013Article
- Structural and biochemical analysis of DNA helix invasion by the bacterial 8-oxoguanine DNA glycosylase MutM.The Journal of biological chemistry · 2013Article
- Recent advances in the structural mechanisms of DNA glycosylases.Biochimica et biophysica acta · 2013Review
- Pulsed electron double resonance in structural studies of spin-labeled nucleic acids.Acta naturae · 2013Article
- DNA repair and genome maintenance in Bacillus subtilis.Microbiology and molecular biology reviews : MMBR · 2012Review
- Structural and biochemical studies of a plant formamidopyrimidine-DNA glycosylase reveal why eukaryotic Fpg glycosylases do not excise 8-oxoguanine.DNA repair · 2012Article
- Thermodynamics of the multi-stage DNA lesion recognition and repair by formamidopyrimidine-DNA glycosylase using pyrrolocytosine fluorescence--stopped-flow pre-steady-state kinetics.Nucleic acids research · 2012Article
- Enforced presentation of an extrahelical guanine to the lesion recognition pocket of human 8-oxoguanine glycosylase, hOGG1.The Journal of biological chemistry · 2012Article
- Sequence-dependent structural variation in DNA undergoing intrahelical inspection by the DNA glycosylase MutM.The Journal of biological chemistry · 2012Article
- Strandwise translocation of a DNA glycosylase on undamaged DNA.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
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5 authors.
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Abstract
MutM, a bacterial DNA glycosylase, protects genome integrity by catalyzing glycosidic bond cleavage of 8-oxoguanine (oxoG) lesions, thereby initiating base excision DNA repair. The process of searching for and locating oxoG lesions is especially challenging, because of the close structural resemblance of oxoG to its million-fold more abundant progenitor, G. Extrusion of the target nucleobase from the DNA double helix to an extrahelical position is an essential step in lesion recognition and catalysis by MutM. Although the interactions between the extruded oxoG and the active site of MutM have been well characterized, little is known in structural detail regarding the interrogation of extruded normal DNA bases by MutM. Here we report the capture and structural elucidation of a complex in which MutM is attempting to present an undamaged G to its active site. The structure of this MutM-extrahelical G complex provides insights into the mechanism MutM employs to discriminate against extrahelical normal DNA bases and into the base extrusion process in general.
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