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- EMDB-2462: Structure and Host Adhesion Mechanism of Virulent Lactococcal Phage p2 -

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Basic information

Entry
Database: EMDB / ID: EMD-2462
TitleStructure and Host Adhesion Mechanism of Virulent Lactococcal Phage p2
Map dataIcosahedral reconstruction of the capsid of lactococcal phage p2.
Sample
  • Sample: Capsid of Lactococcal phage p2
  • Virus: Lactococcus lactis phage p2 (virus)
KeywordsLactococcus lactis / Siphoviridae / 936 phages / Bacteriophage / electron microscopy / single-particle / p2
Biological speciesLactococcus lactis phage p2 (virus)
Methodsingle particle reconstruction / cryo EM / Resolution: 13.0 Å
AuthorsBebeacua C / Tremblay D / Farenc C / Chapot MP / Sadovskaya I / van Heel M / Veesler D / Moineau S / Cambillau C
CitationJournal: J Virol / Year: 2013
Title: Structure, adsorption to host, and infection mechanism of virulent lactococcal phage p2.
Authors: Cecilia Bebeacua / Denise Tremblay / Carine Farenc / Marie-Pierre Chapot-Chartier / Irina Sadovskaya / Marin van Heel / David Veesler / Sylvain Moineau / Christian Cambillau /
Abstract: Lactococcal siphophages from the 936 and P335 groups infect the Gram-positive bacterium Lactococcus lactis using receptor binding proteins (RBPs) attached to their baseplate, a large multiprotein ...Lactococcal siphophages from the 936 and P335 groups infect the Gram-positive bacterium Lactococcus lactis using receptor binding proteins (RBPs) attached to their baseplate, a large multiprotein complex at the distal part of the tail. We have previously reported the crystal and electron microscopy (EM) structures of the baseplates of phages p2 (936 group) and TP901-1 (P335 group) as well as the full EM structure of the TP901-1 virion. Here, we report the complete EM structure of siphophage p2, including its capsid, connector complex, tail, and baseplate. Furthermore, we show that the p2 tail is characterized by the presence of protruding decorations, which are related to adhesins and are likely contributed by the major tail protein C-terminal domains. This feature is reminiscent of the tail of Escherichia coli phage λ and Bacillus subtilis phage SPP1 and might point to a common mechanism for establishing initial interactions with their bacterial hosts. Comparative analyses showed that the architecture of the phage p2 baseplate differs largely from that of lactococcal phage TP901-1. We quantified the interaction of its RBP with the saccharidic receptor and determined that specificity is due to lower k(off) values of the RBP/saccharidic dissociation. Taken together, these results suggest that the infection of L. lactis strains by phage p2 is a multistep process that involves reversible attachment, followed by baseplate activation, specific attachment of the RBPs to the saccharidic receptor, and DNA ejection.
History
DepositionSep 11, 2013-
Header (metadata) releaseSep 25, 2013-
Map releaseSep 25, 2013-
UpdateApr 16, 2014-
Current statusApr 16, 2014Processing site: PDBe / Status: Released

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Structure visualization

Movie
  • Surface view with section colored by density value
  • Surface level: 0.5
  • Imaged by UCSF Chimera
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  • Surface view colored by radius
  • Surface level: 0.5
  • Imaged by UCSF Chimera
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Movie viewer
Structure viewerEM map:
SurfViewMolmilJmol/JSmol
Supplemental images

EMD-2462.png

emd_2462.png

Downloads & links

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Map

FileDownload / File: emd_2462.map.gz / Format: CCP4 / Size: 29.8 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
AnnotationIcosahedral reconstruction of the capsid of lactococcal phage p2.
Voxel sizeX=Y=Z: 3.53 Å
Density
Contour LevelBy AUTHOR: 0.5 / Movie #1: 0.5
Minimum - Maximum-4.54166365 - 7.45390415
Average (Standard dev.)0.08800913 (±0.73049051)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin-100-100-100
Dimensions200200200
Spacing200200200
CellA=B=C: 706.0 Å
α=β=γ: 90.0 °

CCP4 map header:

modeImage stored as Reals
Å/pix. X/Y/Z3.533.533.53
M x/y/z200200200
origin x/y/z0.0000.0000.000
length x/y/z706.000706.000706.000
α/β/γ90.00090.00090.000
start NX/NY/NZ00-40
NX/NY/NZ555581
MAP C/R/S123
start NC/NR/NS-100-100-100
NC/NR/NS200200200
D min/max/mean-4.5427.4540.088

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Supplemental data

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Sample components

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Entire : Capsid of Lactococcal phage p2

EntireName: Capsid of Lactococcal phage p2
Components
  • Sample: Capsid of Lactococcal phage p2
  • Virus: Lactococcus lactis phage p2 (virus)

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Supramolecule #1000: Capsid of Lactococcal phage p2

SupramoleculeName: Capsid of Lactococcal phage p2 / type: sample / ID: 1000 / Oligomeric state: 60-mer / Number unique components: 1
Molecular weightExperimental: 3 MDa / Theoretical: 3 MDa

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Supramolecule #1: Lactococcus lactis phage p2

SupramoleculeName: Lactococcus lactis phage p2 / type: virus / ID: 1 / Name.synonym: Lactococcal phage p2
Details: The capsid was selected from a sample containing entire Lactococcal phages p2.
NCBI-ID: 100641 / Sci species name: Lactococcus lactis phage p2 / Virus type: OTHER / Virus isolate: SPECIES / Virus enveloped: No / Virus empty: No / Syn species name: Lactococcal phage p2
Host (natural)Organism: Lactococcal lactis / Strain: NZ9000 / synonym: BACTERIA(EUBACTERIA)
Virus shellShell ID: 1 / Name: T7 / Diameter: 660 Å / T number (triangulation number): 7

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Experimental details

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Structure determination

Methodcryo EM
Processingsingle particle reconstruction
Aggregation stateparticle

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Sample preparation

BufferpH: 7.5 / Details: 50 mM Tris-HCl, 100 mM NaCl, 8 mM MgSO4
GridDetails: Quantifoil grids
VitrificationCryogen name: ETHANE / Chamber humidity: 100 % / Instrument: FEI VITROBOT MARK I / Method: Blot for 2 seconds before plunging

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Electron microscopy

MicroscopeFEI/PHILIPS CM200T
Electron beamAcceleration voltage: 200 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: SPOT SCAN / Imaging mode: BRIGHT FIELDBright-field microscopy / Cs: 2.2 mm / Nominal defocus max: 0.002 µm / Nominal defocus min: 0.001 µm / Nominal magnification: 50000
Sample stageSpecimen holder model: GATAN LIQUID NITROGEN
Alignment procedureLegacy - Astigmatism: Objective lens astigmatism was corrected at 100,000 times magnification.
DateJul 1, 2009
Image recordingCategory: CCD / Film or detector model: GENERIC TVIPS (4k x 4k) / Digitization - Sampling interval: 3.53 µm / Number real images: 200 / Average electron dose: 10 e/Å2

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Image processing

CTF correctionDetails: Images
Final reconstructionApplied symmetry - Point group: I (icosahedral) / Algorithm: OTHER / Resolution.type: BY AUTHOR / Resolution: 13.0 Å / Resolution method: OTHER / Software - Name: IMAGIC / Number images used: 3329
DetailsReconstruction imposing Icosahedral reconstruction

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Atomic model buiding 1

Initial modelPDB ID:

1ohg

SoftwareName: Chimera
Details60 copies of the hexamer of HK97 MCP were manually fitted and automatically refined with Chimera
RefinementSpace: REAL / Protocol: RIGID BODY FIT

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