Journal
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
Volume 106, Issue 21, Pages 8507-8512Publisher
NATL ACAD SCIENCES
DOI: 10.1073/pnas.0812407106
Keywords
NMR; structure docking; unstructured proteins; virus assembly; virus infection
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Funding
- Biotechnology and Biological Sciences Research Council [BB/F012705/1, B17360] Funding Source: Medline
- BBSRC [BB/F012705/1] Funding Source: UKRI
- Biotechnology and Biological Sciences Research Council [BB/F012705/1, B17360] Funding Source: researchfish
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In many bacterial viruses and in certain animal viruses, the double-stranded DNA genome enters and exits the capsid through a portal gatekeeper. We report a pseudoatomic structure of a complete portal system. The bacteriophage SPP1 gatekeeper is composed of dodecamers of the portal protein gp6, the adaptor gp15, and the stopper gp16. The solution structures of gp15 and gp16 were determined by NMR. They were then docked together with the X-ray structure of gp6 into the electron density of the approximate to 1-MDa SPP1 portal complex purified from DNA-filled capsids. The resulting structure reveals that gatekeeper assembly is accompanied by a large rearrangement of the gp15 structure and by folding of a flexible loop of gp16 to form an intersubunit parallel beta-sheet that closes the portal channel. This stopper system prevents release of packaged DNA. Disulfide cross-linking between beta-strands of the stopper blocks the key conformational changes that control genome ejection from the virus at the beginning of host infection.
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