CHEMICAL STRUCTURE;
CRYSTAL STRUCTURE;
DNA SEQUENCE;
DNA STRUCTURE;
ENZYME CONFORMATION;
ENZYME STRUCTURE;
HYDROGEN BOND;
MOLECULAR RECOGNITION;
NUCLEOTIDE SEQUENCE;
PRIORITY JOURNAL;
PROTEIN DNA INTERACTION;
REVIEW;
DEOXYRIBONUCLEASES, TYPE II SITE-SPECIFIC;
PROTEIN CONFORMATION;
SUPPORT, U.S. GOV'T, P.H.S.;
Linn S.M., Lloyd R.S., Roberts R.J., edn. 2, Cold Spring Harbor Laboratory Press, Cold Spring Harbor, An outstanding review of the entire spectrum of research into type II restriction endonucleases. Essential reading for anyone with interests in enzymes and protein-nucleic acid interactions.
The structure of restriction endonuclease BamHI and its relationship to EcoRI
The structure of BamHI is shown to resemble EcoRI, despite the lack of sequence similarity between the two enzymes. The active site of BamHI is shown to be structurally similar to that of EcoRI and EcoRV, but the mechanism by which BamHI activates a water molecule for nucleophilic attack is proposed to be different.
Structure of restriction endonuclease BamHI phased at 1.95Åresolution by MAD analysis
A detailed description of the BamHI structure, determined to 1.95Åresolution by the multiwavelength anomalous diffraction (MAD) method. Mutants of the enzyme that are deficient in cleavage capacity are shown to map near the DNA-binding cleft. Efforts to detect a common core motif in other endonucleases were unsuccessful.
The crystal structure of PvuII in complex with specific DNA (2.6Å). Like EcoRV, PvuII approaches DNA from the minor groove side but makes the majority of its base pair contacts in the major groove. These contacts are mediated by two antiparallel ß-strands. The DNA maintains a B-DNA like conformation, proving that distortion is not a prerequisite for specific complex formation. The catalytic region of PvuII is shown to be similar to that of EcoRV, EcoRI, and BamHI.
Crystal structure of PvuII endonuclease reveals extensive homologies to EcoRV
The crystal structure of PvuII (2.4Å) determined in the absence of DNA. The DNA-binding subdomains of PvuII and EcoRV are shown to be structurally related, despite the lack of sequence homology between the two enzymes. Potential catalytic residues are deduced from the structural similarity to EcoRV.
Accuracy of the EcoRI restriction endonuclease: binding and cleavage studies with oligodeoxynucleotide substrates containing degenerate recognition sequences
Facilitated distortion of the DNA site enhances EcoRI endonuclease-DNA recognition
edn 1, Following from their earlier work [13], the authors use purine base analogs to measure the energetic costs of deleting hydrogen bonds between EcoRI and its recognition sequence.
Substrate-assisted catalysis in the cleavage of DNA by the EcoRI and EcoRV restriction enzymes
edn 1, Experimental evidence is presented to support the notion that the phosphate group 3′ to the scissile phosphodiester activates the attacking water molecule.
