4KFT

Structure of the genome packaging NTPase B204 from Sulfolobus turreted icosahedral virus 2 in complex with ATP-gammaS

4KFT の概要

• エントリーDOI: 10.2210/pdb4kft/pdb
• 関連するPDBエントリー: 4KFR 4KFS 4KFU
• 分子名称: Genome packaging NTPase B204, PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER, MAGNESIUM ION, ... (7 entities in total)
• 機能のキーワード: ftsk-hera superfamily, p-loop atpase, genome packaging ntpase, hydrolase
• 由来する生物種: Sulfolobus turreted icosahedral virus 2 (STIV2)
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 103923.07

構造登録者

Happonen, L.J.,Oksanen, E.,Kajander, T.,Goldman, A.,Butcher, S. (登録日: 2013-04-27, 公開日: 2013-05-22, 最終更新日: 2023-09-20)

主引用文献

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

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: 23698307
DOI: 10.1128/JVI.00831-13

実験手法

X-RAY DIFFRACTION (2.241 Å)