The Structure of the NTPase That Powers DNA Packaging into Sulfolobus Turreted Icosahedral Virus 2
(2013) In Journal of Virology 87(15). p.8388-8398- 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... (More)
- 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. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/4042816
- author
- Happonen, Lotta ; Oksanen, Esko LU ; Liljeroos, Lassi ; Goldman, Adrian ; Kajander, Tommi and Butcher, Sarah J.
- organization
- publishing date
- 2013
- type
- Contribution to journal
- publication status
- published
- subject
- in
- Journal of Virology
- volume
- 87
- issue
- 15
- pages
- 8388 - 8398
- publisher
- American Society for Microbiology
- external identifiers
-
- wos:000321590200012
- scopus:84880576754
- pmid:23698307
- ISSN
- 1098-5514
- DOI
- 10.1128/JVI.00831-13
- language
- English
- LU publication?
- yes
- id
- ab46afb3-2c83-405e-92b7-166ab17dad61 (old id 4042816)
- date added to LUP
- 2016-04-01 14:00:50
- date last changed
- 2022-01-27 22:22:31
@article{ab46afb3-2c83-405e-92b7-166ab17dad61, 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.}}, author = {{Happonen, Lotta and Oksanen, Esko and Liljeroos, Lassi and Goldman, Adrian and Kajander, Tommi and Butcher, Sarah J.}}, issn = {{1098-5514}}, language = {{eng}}, number = {{15}}, pages = {{8388--8398}}, publisher = {{American Society for Microbiology}}, series = {{Journal of Virology}}, title = {{The Structure of the NTPase That Powers DNA Packaging into Sulfolobus Turreted Icosahedral Virus 2}}, url = {{http://dx.doi.org/10.1128/JVI.00831-13}}, doi = {{10.1128/JVI.00831-13}}, volume = {{87}}, year = {{2013}}, }