Advanced

The Structure of the NTPase That Powers DNA Packaging into Sulfolobus Turreted Icosahedral Virus 2

Happonen, Lotta ; Oksanen, Esko LU ; Liljeroos, Lassi ; Goldman, Adrian ; Kajander, Tommi and Butcher, Sarah J. (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:
author
; ; ; ; and
organization
publishing date
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
2020-10-20 03:39:06
@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},
}