Article
Two distinct modes of metal ion binding in the nuclease active site of a viral DNA-packaging terminase: insight into the two-metal-ion catalytic mechanism.
Nucleic acids research - 15 Dec 2015
Zhao Haiyan, Lin Zihan, Lynn Anna Y, Varnado Brittany, Beutler John A, Murelli Ryan P, Le Grice Stuart F J, Tang Liang
Abstract excerpt
Many dsDNA viruses encode DNA-packaging terminases, each containing a nuclease domain that resolves concatemeric DNA into genome-length units. Terminase nucleases resemble the RNase H-superfamily nucleotidyltransferases in folds, and share a two-metal-ion catalytic mechanism. Here we show that residue K428 of a bacteriophage terminase gp2 nuclease domain mediates binding of the metal cofactor Mg(2+). A K428A...
Read the complete abstract on PubMedTopics
Share this publication in a Topic to start or enrich a Post.