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The Structure of th...
The Structure of the NTPase That Powers DNA Packaging into Sulfolobus Turreted Icosahedral Virus 2
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Happonen, Lotta (författare)
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- Oksanen, Esko (författare)
- Lund University,Lunds universitet,European Spallation Source ESS AB,Stiftelser och övriga anknutna verksamheter,Other Institutions and Utilities
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Liljeroos, Lassi (författare)
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Goldman, Adrian (författare)
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Kajander, Tommi (författare)
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Butcher, Sarah J. (författare)
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(creator_code:org_t)
- 2013
- 2013
- Engelska.
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Ingår i: Journal of Virology. - 1098-5514. ; 87:15, s. 8388-8398
- Relaterad länk:
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http://dx.doi.org/10...
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https://lup.lub.lu.s...
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https://doi.org/10.1...
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Abstract
Ämnesord
Stäng
- 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.
Ämnesord
- NATURVETENSKAP -- Fysik (hsv//swe)
- NATURAL SCIENCES -- Physical Sciences (hsv//eng)
Publikations- och innehållstyp
- art (ämneskategori)
- ref (ämneskategori)
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