Structures of the phage Sf6 large terminase provide new insights into DNA translocation and cleavage

• DOI: 10.1073/pnas.1301133110
• Publication Date: 2013-04-30T04:27:35Z
• Authors: Haiyan Zhao; Theodore E. Chris...; Yvonne N. Kamau; Liang Tang
• Keywords: Nuclease; Linker; Cleave; Molecular motor; Cleavage (geology); RNase H

Many DNA viruses use powerful molecular motors to cleave concatemeric viral into genome-length units and package them preformed procapsid powered by ATP hydrolysis. Here we report the structures of DNA-packaging motor gp2 bacteriophage Sf6, which reveal a unique clade RecA-like ATPase domain an RNase H-like nuclease tethered regulatory linker domain, exhibiting strikingly distinct arrangement. The complexed with nucleotides reveal, at atomic detail, catalytic center embraced domain. activity is modulated stimulated ATP. An extended DNA-binding surface formed These results suggest mechanism for translation chemical reaction physical motion provide insights coordination translocation cleavage in motor, may be achieved via linker-domain–mediated interdomain communication driven