ArticleThe Journal of biological chemistry2010
Structural and dynamic features of the MutT protein in the recognition of nucleotides with the mutagenic 8-oxoguanine base.
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 25 papers.
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Who cites it
25 citing papers in PubMed, 45 citations in OpenAlex.
- Article
- Neutron and time-resolved X-ray crystallography reveal the substrate recognition and catalytic mechanism of human Nudix hydrolase MTH1.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Split MutT prevents the mutator phenotype of mutT-deficient Escherichia coli.Genes and environment : the official journal of the Japanese Environmental Mutagen Society · 2024Article
- Visualization of oxidized guanine nucleotides accumulation in living cells with split MutT.Nucleic acids research · 2024Article
- Noncatalytic Domains in DNA Glycosylases.International journal of molecular sciences · 2022Review
- Visualizing the three-metal-ion-dependent cleavage of a mutagenic nucleotide.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Visualization of mutagenic nucleotide processing byProceedings of the National Academy of Sciences of the United States of America · 2022Article
- Review
- Structure of the mammalian adenine DNA glycosylase MUTYH: insights into the base excision repair pathway and cancer.Nucleic acids research · 2021Article
- Beyond Chelation: EDTA Tightly Binds Taq DNA Polymerase, MutT and dUTPase and Directly Inhibits dNTPase Activity.Biomolecules · 2019Article
- A cryptic activity in the Nudix hydrolase superfamily.Protein science : a publication of the Protein Society · 2019Article
- The evolution of function within the Nudix homology clan.Proteins · 2017Article
- Structural and Kinetic Studies of the Human Nudix Hydrolase MTH1 Reveal the Mechanism for Its Broad Substrate Specificity.The Journal of biological chemistry · 2017Article
- Article
- Insights into the substrate specificity of the MutT pyrophosphohydrolase using structural analogues of 8-oxo-2'-deoxyguanosine nucleotide.Bioorganic & medicinal chemistry letters · 2016Article
- The BER necessities: the repair of DNA damage in human-adapted bacterial pathogens.Nature reviews. Microbiology · 2015Review
- MutT from the fish pathogen Aliivibrio salmonicida is a cold-active nucleotide-pool sanitization enzyme with unexpectedly high thermostability.FEBS open bio · 2015Article
- Mycobacterium tuberculosis MutT1 (Rv2985) and ADPRase (Rv1700) proteins constitute a two-stage mechanism of 8-oxo-dGTP and 8-oxo-GTP detoxification and adenosine to cytidine mutation avoidance.The Journal of biological chemistry · 2013Article
- Mechanism for KRIT1 release of ICAP1-mediated suppression of integrin activation.Molecular cell · 2013Article
- Substrate ambiguity among the nudix hydrolases: biologically significant, evolutionary remnant, or both?Cellular and molecular life sciences : CMLS · 2013Article
Corrections and comments
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Authors and funding
13 authors at 5 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Escherichia coli MutT hydrolyzes 8-oxo-dGTP to 8-oxo-dGMP, an event that can prevent the misincorporation of 8-oxoguanine opposite adenine in DNA. Of the several enzymes that recognize 8-oxoguanine, MutT exhibits high substrate specificity for 8-oxoguanine nucleotides; however, the structural basis for this specificity is unknown. The crystal structures of MutT in the apo and holo forms and in the binary and ternary forms complexed with the product 8-oxo-dGMP and 8-oxo-dGMP plus Mn(2+), respectively, were determined. MutT strictly recognizes the overall conformation of 8-oxo-dGMP through a number of hydrogen bonds. This recognition mode revealed that 8-oxoguanine nucleotides are discriminated from guanine nucleotides by not only the hydrogen bond between the N7-H and Odelta (N119) atoms but also by the syn glycosidic conformation that 8-oxoguanine nucleotides prefer. Nevertheless, these discrimination factors cannot by themselves explain the roughly 34,000-fold difference between the affinity of MutT for 8-oxo-dGMP and dGMP. When the binary complex of MutT with 8-oxo-dGMP is compared with the ligand-free form, ordering and considerable movement of the flexible loops surrounding 8-oxo-dGMP in the binary complex are observed. These results indicate that MutT specifically recognizes 8-oxoguanine nucleotides by the ligand-induced conformational change.
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