4KFS
Structure of the genome packaging NTPase B204 from Sulfolobus turreted icosahedral virus 2 in complex with AMP
Summary for 4KFS
| Entry DOI | 10.2210/pdb4kfs/pdb |
| Related | 4KFR 4KFT 4KFU |
| Descriptor | Genome packaging NTPase B204, ADENOSINE MONOPHOSPHATE, ZINC ION, ... (7 entities in total) |
| Functional Keywords | ftsk-hera superfamily, p-loop atpase, genome packaging ntpase, hydrolase |
| Biological source | Sulfolobus turreted icosahedral virus 2 (STIV2) |
| Total number of polymer chains | 2 |
| Total formula weight | 50751.01 |
| Authors | Happonen, L.J.,Oksanen, E.,Kajander, T.,Goldman, A.,Butcher, S. (deposition date: 2013-04-27, release date: 2013-05-22, Last modification date: 2023-09-20) |
| Primary citation | Happonen, L.J.,Oksanen, E.,Liljeroos, L.,Goldman, A.,Kajander, T.,Butcher, S.J. The Structure of the NTPase That Powers DNA Packaging into Sulfolobus Turreted Icosahedral Virus 2. J.Virol., 87:8388-8398, 2013 Cited by PubMed Abstract: Biochemical reactions powered by ATP hydrolysis are fundamental for the movement of molecules and cellular structures. One such reaction is the encapsidation of the double-stranded DNA (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 nontailed, membrane-containing, hyperthermoacidophilic archaeal dsDNA virus Sulfolobus turreted icosahedral virus 2. These are the first structures of a genome-packaging NTPase from a nontailed, 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°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 DNA-translocating mechanism. PubMed: 23698307DOI: 10.1128/JVI.00831-13 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.946 Å) |
Structure validation
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