Article
Fine tuning of the catalytic activity of colicin E7 nuclease domain by systematic N-terminal mutations.
Protein science : a publication of the Protein Society - 1 Aug 2014
Németh Eszter, Körtvélyesi Tamás, Thulstrup Peter W, Christensen Hans E M, Kožíšek Milan, Nagata Kyosuke, Czene Anikó, Gyurcsik Béla
Abstract excerpt
The nuclease domain of colicin E7 (NColE7) promotes the nonspecific cleavage of nucleic acids at its C-terminal HNH motif. Interestingly, the deletion of four N-terminal residues (446-449 NColE7 = KRNK) resulted in complete loss of the enzyme activity. R447A mutation was reported to decrease the nuclease activity, but a detailed analysis of the role of the highly positive and flexible N-terminus is still missing....
Topics
- Biocatalysis
- Calorimetry
- Circular Dichroism
- Colicins
- Crystallography, X-Ray
- Enzyme Activation
- Models, Molecular
- Molecular Dynamics Simulation
- Mutation
- Nucleic Acids
- Protein Structure, Tertiary
- Quantum Theory
