S. et al. The crystal structure of the nuclease domain of colicin E7 suggests a mechanism for binding to double-stranded DNA by the H-N-H endonucleases. J Mol Biol 324, 227–236 (2002). 8. Pommer, A. J. et al. Mechanism and cleavage specificity of the H-N-H endonuclease colicin ...
The crystal structure of the nuclease domain of ColE7 in complex with a duplex DNA has been determined at 2.5 resolution. The HNH motif is bound at the minor groove primarily to DNA phosphate groups at and beyond the 3′ side of the scissile phosphate, with little interaction with ribose ...
Colicin E7 is a representative member of this family containing the strictly conserved HNH motif at its C-terminus. Structural and biochemical studies suggested that the HNH motif could contain all the residues necessary for metal ion binding and nuclease activity. In this work a 43 amino acid ...
Comparison of the glutathion-S-transferase-fused N-terminal deletion mutants of the colicin \\{E7\\} nuclease domain suggested that the presence of the DNA-binding site is still not sufficient for the catalytic activity.Béla Gyurcsik and Anikó Czene and Hajnalka Jankovics and Noémi I. Jakab-...