ArticleNucleic acids research2009
Structural mechanisms for the 5'-CCWGG sequence recognition by the N- and C-terminal domains of EcoRII.
Article in Nucleic acids research, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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22 citing papers in PubMed, 40 citations in OpenAlex.
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- Complete Genome Sequence of a Multidrug-Resistant Strain, Escherichia coli ATCC BAA-196, as a Model for Studying Induced Antibiotic Resistance Reversion.Microbiology resource announcements · 2019Article
- Unique mechanism of target recognition by PfoI restriction endonuclease of the CCGG-family.Nucleic acids research · 2019Article
- The crystal structure of theThe Journal of biological chemistry · 2018Article
- Structural basis of DNA target recognition by the B3 domain of Arabidopsis epigenome reader VAL1.Nucleic acids research · 2018Article
- Behavior of BsoBI endonuclease in the presence and absence of DNA.Journal of molecular modeling · 2017Article
- UbaLAI is a monomeric Type IIE restriction enzyme.Nucleic acids research · 2017Article
- Restriction endonuclease AgeI is a monomer which dimerizes to cleave DNA.Nucleic acids research · 2017Article
- Functional significance of protein assemblies predicted by the crystal structure of the restriction endonuclease BsaWI.Nucleic acids research · 2015Article
- Crystal structure of the R-protein of the multisubunit ATP-dependent restriction endonuclease NgoAVII.Nucleic acids research · 2014Article
- Type II restriction endonucleases--a historical perspective and more.Nucleic acids research · 2014Review
- Structural insight into the specificity of the B3 DNA-binding domains provided by the co-crystal structure of the C-terminal fragment of BfiI restriction enzyme.Nucleic acids research · 2014Article
- The Arabidopsis B3 domain protein VERNALIZATION1 (VRN1) is involved in processes essential for development, with structural and mutational studies revealing its DNA-binding surface.The Journal of biological chemistry · 2013Article
- Structural mechanisms of the degenerate sequence recognition by Bse634I restriction endonuclease.Nucleic acids research · 2012Article
- Re-visiting protein-centric two-tier classification of existing DNA-protein complexes.BMC bioinformatics · 2012Article
- Systematic analysis of plant-specific B3 domain-containing proteins based on the genome resources of 11 sequenced species.Molecular biology reports · 2012Article
- Type III restriction endonuclease EcoP15I is a heterotrimeric complex containing one Res subunit with several DNA-binding regions and ATPase activity.Nucleic acids research · 2012Article
- DNA intercalation without flipping in the specific ThaI-DNA complex.Nucleic acids research · 2011Article
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Authors and funding
5 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
EcoRII restriction endonuclease is specific for the 5'-CCWGG sequence (W stands for A or T); however, it shows no activity on a single recognition site. To activate cleavage it requires binding of an additional target site as an allosteric effector. EcoRII dimer consists of three structural units: a central catalytic core, made from two copies of the C-terminal domain (EcoRII-C), and two N-terminal effector DNA binding domains (EcoRII-N). Here, we report DNA-bound EcoRII-N and EcoRII-C structures, which show that EcoRII combines two radically different structural mechanisms to interact with the effector and substrate DNA. The catalytic EcoRII-C dimer flips out the central T:A base pair and makes symmetric interactions with the CC:GG half-sites. The EcoRII-N effector domain monomer binds to the target site asymmetrically in a single defined orientation which is determined by specific hydrogen bonding and van der Waals interactions with the central T:A pair in the major groove. The EcoRII-N mode of the target site recognition is shared by the large class of higher plant transcription factors of the B3 superfamily.
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