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TitleStructure of lactococcal phage p2 baseplate and its mechanism of activation.
Journal, issue, pagesProc Natl Acad Sci U S A, Vol. 107, Issue 15, Page 6852-6857, Year 2010
Publish dateApr 13, 2010
AuthorsGiuliano Sciara / Cecilia Bebeacua / Patrick Bron / Denise Tremblay / Miguel Ortiz-Lombardia / Julie Lichière / Marin van Heel / Valérie Campanacci / Sylvain Moineau / Christian Cambillau /
PubMed AbstractSiphoviridae is the most abundant viral family on earth which infects bacteria as well as archaea. All known siphophages infecting gram+ Lactococcus lactis possess a baseplate at the tip of their ...Siphoviridae is the most abundant viral family on earth which infects bacteria as well as archaea. All known siphophages infecting gram+ Lactococcus lactis possess a baseplate at the tip of their tail involved in host recognition and attachment. Here, we report analysis of the p2 phage baseplate structure by X-ray crystallography and electron microscopy and propose a mechanism for the baseplate activation during attachment to the host cell. This approximately 1 MDa, Escherichia coli-expressed baseplate is composed of three protein species, including six trimers of the receptor-binding protein (RBP). RBPs host-recognition domains point upwards, towards the capsid, in agreement with the electron-microscopy map of the free virion. In the presence of Ca(2+), a cation mandatory for infection, the RBPs rotated 200 degrees downwards, presenting their binding sites to the host, and a channel opens at the bottom of the baseplate for DNA passage. These conformational changes reveal a novel siphophage activation and host-recognition mechanism leading ultimately to DNA ejection.
External linksProc Natl Acad Sci U S A / PubMed:20351260 / PubMed Central
MethodsEM (single particle) / X-ray diffraction
Resolution2.6 - 26.0 Å
Structure data

EMDB-1699:
Structure of Lactococcal Phage p2 Baseplate and its Mechanism of Activation
Method: EM (single particle) / Resolution: 22.0 Å

EMDB-1706:
Cryo-EM map of Lactococcal phage p2 baseplate consisting of ORF 15, 16 and 18.
Method: EM (single particle) / Resolution: 26.0 Å

PDB-2wzp:
Structures of Lactococcal Phage p2 Baseplate Shed Light on a Novel Mechanism of Host Attachment and Activation in Siphoviridae
Method: X-RAY DIFFRACTION / Resolution: 2.6 Å

PDB-2x53:
Structure of the phage p2 baseplate in its activated conformation with Sr
Method: X-RAY DIFFRACTION / Resolution: 3.9 Å

PDB-4v5i:
Structure of the Phage P2 Baseplate in its Activated Conformation with Ca
Method: X-RAY DIFFRACTION / Resolution: 5.464 Å

Chemicals

ChemComp-HOH:
WATER

ChemComp-SR:
STRONTIUM ION

ChemComp-CA:
Unknown entry

Source
  • lactococcus phage p2 (virus)
  • Lactococcus lactis phage p2 (virus)
  • lama glama (llama)
KeywordsVIRAL PROTEIN / BASEPLATE / SIPHOVIRIDAE / LACTOCOCCUS LACTIS

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