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Publication Abstract from PubMed

Biochemical reactions powered by ATP hydrolysis are fundamental for the movement of molecules and cellular structures. One such reaction is the encapsidation of the dsDNA genome of an icosahedrally-symmetric virus into a preformed procapsid with the help of a genome translocating NTPase. Such NTPases have been characterized in detail from both RNA and tailed DNA viruses. We present four crystal structures and the biochemical activity of a thermophilic NTPase, B204, from the non-tailed, membrane-containing, hyperthermo-acidophilic archaeal dsDNA virus Sulfolobus turreted icosahedral virus 2. These are the first structures of a genome packaging NTPase from a non-tailed, dsDNA virus with an archaeal host. The four structures highlight the catalytic cycle of B204, pinpointing the molecular movement between substrate-bound (open) and empty (closed) active sites. The protein is shown to bind both single-stranded and double-stranded nucleic acids, and to have an optimum activity at 80 degrees C and pH 4.5. The overall fold of B204 places it in the FtsK-HerA superfamily of P-loop ATPases, whose cellular and viral members have been suggested to share a common DNA-translocating mechanism.

The structure of the NTPase that powers DNA packaging into Sulfolobus turreted icosahedral virus 2.,Happonen LJ, Oksanen E, Liljeroos L, Goldman A, Kajander T, Butcher SJ J Virol. 2013 May 22. PMID:23698307^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.