Portal protein: Difference between revisions
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== Function == | == Function == | ||
The '''portal protein''' (PP) is a key component during viral chromosomal packaging. PPs have a central channel through which DNA movements occur. PPs are proposed to be the mechanical device that pumps DNA to the interior of the viral capsid<ref>PMID:15110523</ref>. The DNA translocation motor is composed of PP and of the the viral ATPase that fuels DNA translocation. The PP has an active control over the viral ATPase activity<ref>PMID:16735502</ref>. | The '''portal protein''' (PP) is a key component during viral chromosomal packaging. PPs have a central channel through which DNA movements occur. PPs are proposed to be the mechanical device that pumps DNA to the interior of the viral capsid<ref>PMID:15110523</ref>. The DNA translocation motor is composed of PP and of the the viral ATPase that fuels DNA translocation. The PP has an active control over the viral ATPase activity<ref>PMID:16735502</ref>. | ||
== 3D Structures of portal protein == | |||
[[Portal protein 3D structures]] | |||
</StructureSection> | </StructureSection> | ||
Revision as of 11:30, 5 September 2023
FunctionThe portal protein (PP) is a key component during viral chromosomal packaging. PPs have a central channel through which DNA movements occur. PPs are proposed to be the mechanical device that pumps DNA to the interior of the viral capsid[1]. The DNA translocation motor is composed of PP and of the the viral ATPase that fuels DNA translocation. The PP has an active control over the viral ATPase activity[2]. 3D Structures of portal protein |
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3D Structures of portal protein3D Structures of portal protein
Updated on 05-September-2023
ReferencesReferences
- ↑ Isidro A, Henriques AO, Tavares P. The portal protein plays essential roles at different steps of the SPP1 DNA packaging process. Virology. 2004 May 1;322(2):253-63. doi: 10.1016/j.virol.2004.02.012. PMID:15110523 doi:http://dx.doi.org/10.1016/j.virol.2004.02.012
- ↑ Oliveira L, Henriques AO, Tavares P. Modulation of the viral ATPase activity by the portal protein correlates with DNA packaging efficiency. J Biol Chem. 2006 Aug 4;281(31):21914-23. doi: 10.1074/jbc.M603314200. Epub 2006 , May 30. PMID:16735502 doi:http://dx.doi.org/10.1074/jbc.M603314200