1pt3
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Crystal structures of nuclease-ColE7 complexed with octamer DNA
OverviewOverview
The bacterial toxin ColE7 bears an HNH motif which has been identified in, hundreds of prokaryotic and eukaryotic endonucleases, involved in DNA, homing, restriction, repair, or chromosome degradation. The crystal, structure of the nuclease domain of ColE7 in complex with a duplex DNA has, been determined at 2.5 A 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 groups and bases., This result provides a structural basis for sugar- and, sequence-independent DNA recognition and the inhibition mechanism by, inhibitor Im7, which blocks the substrate binding site but not the active, site. Structural comparison shows that two families of endonucleases bind, and bend DNA in a similar way to that of the HNH ColE7, indicating that, endonucleases containing a "betabetaalpha-metal" fold of active site, possess a universal mode for protein-DNA interactions.
About this StructureAbout this Structure
1PT3 is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
ReferenceReference
DNA binding and degradation by the HNH protein ColE7., Hsia KC, Chak KF, Liang PH, Cheng YS, Ku WY, Yuan HS, Structure. 2004 Feb;12(2):205-14. PMID:14962381
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