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Structure of a viral DNA gatekeeper at 10 angstrom resolution by cryo-electron microscopy

MPG-Autoren
http://pubman.mpdl.mpg.de/cone/persons/resource/persons50138

Dröge,  Anja
Dept. of Vertebrate Genomics (Head: Hans Lehrach), Max Planck Institute for Molecular Genetics, Max Planck Society;

http://pubman.mpdl.mpg.de/cone/persons/resource/persons50575

Stiege,  Asita
Research Group Development & Disease (Head: Stefan Mundlos), Max Planck Institute for Molecular Genetics, Max Planck Society;

Weise,  Frank
Max Planck Society;

Lurz,  Rudi
Max Planck Society;

Tavares,  Paulo
Max Planck Society;

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Zitation

Orlova, E. V., Gowen, B., Dröge, A., Stiege, A., Weise, F., Lurz, R., et al. (2003). Structure of a viral DNA gatekeeper at 10 angstrom resolution by cryo-electron microscopy. EMBO Journal, 22(6), 1255-1262.


Zitierlink: http://hdl.handle.net/11858/00-001M-0000-0010-8A84-6
Zusammenfassung
In tailed bacteriophages and herpes viruses, the viral DNA is packaged through the portal protein channel. Channel closure is essential to prevent DNA release after packaging. Here we present the connector structure from bacteriophage SPP1 using cryo-electron microscopy and single particle analysis. The multiprotein complex comprises the portal protein gp6 and the head completion proteins gp15 and gp16. Although we show that gp6 in the connector has a fold similar to that of the isolated portal protein, we observe conformational changes in the region of gp6 exposed to the DNA-packaging ATPase and to gp15. This reorganization does not cause closure of the channel. The connector channel traverses the full height of gp6 and gp15, but it is closed by gp16 at the bottom of the complex. Gp16 acts as a valve whose closure prevents DNA leakage, while its opening is required for DNA release upon interaction of the virus with its host.