Portal protein

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<StructureSection load='2jes' size='340' side='right' caption='Caption for this structure' scene=''>
<StructureSection load='2jes' size='340' side='right' caption='Caption for this structure' scene=''>
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== Function ==
== Function ==
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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>.
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</StructureSection>
</StructureSection>
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== References ==
== References ==
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<references/>
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[[Category:Topic Page]]

Revision as of 10:17, 17 January 2018

Caption for this structure

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3D Structures of portal protein

Updated on 17-January-2018

References

  1. 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
  2. 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

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Michal Harel, Jaime Prilusky

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