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TitleStructure and molecular assignment of lactococcal phage TP901-1 baseplate.
Journal, issue, pagesJ Biol Chem, Vol. 285, Issue 50, Page 39079-39086, Year 2010
Publish dateDec 10, 2010
AuthorsCecilia Bebeacua / Patrick Bron / Livia Lai / Christina Skovgaard Vegge / Lone Brøndsted / Silvia Spinelli / Valérie Campanacci / David Veesler / Marin van Heel / Christian Cambillau /
PubMed AbstractP335 lactococcal phages infect the gram(+) bacterium Lactococcus lactis using a large multiprotein complex located at the distal part of the tail and termed baseplate (BP). The BP harbors the ...P335 lactococcal phages infect the gram(+) bacterium Lactococcus lactis using a large multiprotein complex located at the distal part of the tail and termed baseplate (BP). The BP harbors the receptor-binding proteins (RBPs), which allow the specific recognition of saccharidic receptors localized on the host cell surface. We report here the electron microscopic structure of the phage TP901-1 wild-type BP as well as those of two mutants bppL (-) and bppU(-), lacking BppL (the RBPs) or both peripheral BP components (BppL and BppU), respectively. We also achieved an electron microscopic reconstruction of a partial BP complex, formed by BppU and BppL. This complex exhibits a tripod shape and is composed of nine BppLs and three BppUs. These structures, combined with light-scattering measurements, led us to propose that the TP901-1 BP harbors six tripods at its periphery, located around the central tube formed by ORF46 (Dit) hexamers, at its proximal end, and a ORF47 (Tal) trimer at its distal extremity. A total of 54 BppLs (18 RBPs) are thus available to mediate host anchoring with a large apparent avidity. TP901-1 BP exhibits an infection-ready conformation and differs strikingly from the lactococcal phage p2 BP, bearing only 6 RBPs, and which needs a conformational change to reach its activated state. The comparison of several Siphoviridae structures uncovers a close organization of their central BP core whereas striking differences occur at the periphery, leading to diverse mechanisms of host recognition.
External linksJ Biol Chem / PubMed:20937834 / PubMed Central
MethodsEM (single particle) / X-ray diffraction
Resolution1.85 - 28.0 Å
Structure data

EMDB-1792:
EM map of TP901-1 BppU-BppL complex
Method: EM (single particle) / Resolution: 24.8 Å

EMDB-1793:
The three-dimensional reconstruction of the baseplate of wild-type TP901-1
Method: EM (single particle) / Resolution: 25.0 Å

EMDB-1794:
The three-dimensional reconstruction of the baseplate of TP901-1 bppL mutant
Method: EM (single particle) / Resolution: 25.0 Å

EMDB-1795:
The three-dimensional reconstruction of the baseplate of TP901-1 bppU mutant
Method: EM (single particle) / Resolution: 28.0 Å

PDB-3ejc:
Full length Receptor Binding Protein from Lactococcal phage TP901-1
Method: X-RAY DIFFRACTION / Resolution: 1.85 Å

Chemicals

ChemComp-HOH:
WATER / Water

Source
  • lactococcus phage tp901-1 (virus)
KeywordsVIRAL PROTEIN / SUGAR BINDING PROTEIN / Lactococcus lactis / siphoviridae / receptor binding protein / phage TP901-1 / P335 species

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