ArticleNucleic acids research2014
Crystal structure of the 5hmC specific endonuclease PvuRts1I.
Article in Nucleic acids research, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed, 30 citations in OpenAlex.
- Biology of host-dependent restriction-modification in prokaryotes.EcoSal Plus · 2025Review
- Structural analysis of the BisI family of modification dependent restriction endonucleases.Nucleic acids research · 2024Article
- Characterization of winged helix domain fusion endonucleases as N6-methyladenine-dependent type IV restriction systems.Frontiers in microbiology · 2024Article
- Navigating the pitfalls of mapping DNA and RNA modifications.Nature reviews. Genetics · 2023Review
- Crystal structures of the EVE-HNH endonuclease VcaM4I in the presence and absence of DNA.Nucleic acids research · 2021Article
- Structure-Based Deep Mining Reveals First-Time Annotations for 46 Percent of the Dark Annotation Space of the 9,671-Member Superproteome of the Nucleocytoplasmic Large DNA Viruses.Journal of virology · 2020Article
- The N-terminal domain of Staphylothermus marinus McrB shares structural homology with PUA-like RNA binding proteins.Journal of structural biology · 2020Article
- Protein Domain Guided Screen for Sequence Specific and Phosphorothioate-Dependent Restriction Endonucleases.Frontiers in microbiology · 2020Article
- Crystal structure of the EcoKMcrA N-terminal domain (NEco): recognition of modified cytosine bases without flipping.Nucleic acids research · 2019Article
- A protein architecture guided screen for modification dependent restriction endonucleases.Nucleic acids research · 2019Article
- Structural basis for the recognition of sulfur in phosphorothioated DNA.Nature communications · 2018Article
- Crystal structure of the modification-dependent SRA-HNH endonuclease TagI.Nucleic acids research · 2018Article
- Activity and structure of EcoKMcrA.Nucleic acids research · 2018Article
- The crystal structure of theThe Journal of biological chemistry · 2018Article
- Mechanistic insights into the recognition of 5-methylcytosine oxidation derivatives by the SUVH5 SRA domain.Scientific reports · 2016Article
- Phylogenomics and sequence-structure-function relationships in the GmrSD family of Type IV restriction enzymes.BMC bioinformatics · 2015Article
- Structure-guided sequence specificity engineering of the modification-dependent restriction endonuclease LpnPI.Nucleic acids research · 2015Article
- Expression and purification of a single-chain Type IV restriction enzyme Eco94GmrSD and determination of its substrate preference.Scientific reports · 2015Article
- Recognition and cleavage of 5-methylcytosine DNA by bacterial SRA-HNH proteins.Nucleic acids research · 2015Article
- Modification-dependent restriction endonuclease, MspJI, flips 5-methylcytosine out of the DNA helix.Nucleic acids research · 2014Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
PvuRts1I is a prototype for a larger family of restriction endonucleases that cleave DNA containing 5-hydroxymethylcytosine (5hmC) or 5-glucosylhydroxymethylcytosine (5ghmC), but not 5-methylcytosine (5mC) or cytosine. Here, we report a crystal structure of the enzyme at 2.35 Å resolution. Although the protein has been crystallized in the absence of DNA, the structure is very informative. It shows that PvuRts1I consists of an N-terminal, atypical PD-(D/E)XK catalytic domain and a C-terminal SRA domain that might accommodate a flipped 5hmC or 5ghmC base. Changes to predicted catalytic residues of the PD-(D/E)XK domain or to the putative pocket for a flipped base abolish catalytic activity. Surprisingly, fluorescence changes indicative of base flipping are not observed when PvuRts1I is added to DNA substrates containing pyrrolocytosine in place of 5hmC (5ghmC). Despite this caveat, the structure suggests a model for PvuRts1I activity and presents opportunities for protein engineering to alter the enzyme properties for biotechnological applications.
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