VcaM4I restriction endonuclease in the absence of DNA

Crystal structures of the EVE-HNH endonuclease VcaM4I in the presence and absence of DNA.

A protein architecture guided screen for modification dependent restriction endonucleases.

Protein (7.2 mg/ml) in 0.27 M NaCl, 13.5 mM Tris-HCl pH 8.5, 0.2 M sodium malonate and 0.9 mM TCEP was mixed in 1:1 ratio with reservoir solution (1.8 M ammonium sulfate, 0.1 M MES pH 5.25). Perfluoropolyether oil was used as a cryoprotectant.

Crystal Structure of Human THYN1 protein in complex with 5-methylcytosine containing DNA

CRYSTAL STRUCTURE OF VCAM4I RESTRICTION ENDONUCLEASE IN THE PRESENCE OF 5HMC-MODIFIED SSDNA

CRYSTAL STRUCTURE OF VCAM4I RESTRICTION ENDONUCLEASE IN THE PRESENCE OF 5MC-MODIFIED SSDNA

CRYSTAL STRUCTURE OF VCAM4I RESTRICTION ENDONUCLEASE IN THE PRESENCE OF 5MC-MODIFIED DSDNA

HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
U VALUES : WITH TLS ADDED
THE IDENTITY OF THE SOLVENT MOLECULES HAS BEEN ASSIGNED TENTATIVELY.

The modification specific VcaM4I restriction endonuclease is active as a dimer (each protomer cleaves one strand of the double stranded DNA substrate). The C-terminal HNH nuclease domains mediate the dimerization. The N-terminal EVE domains are responsible for the modification specificity.

PUA superfamily, EVE domain, DNA endonuclease, modification-dependent restriction endonuclease, MDRE, single stranded DNA, HYDROLASE