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- EMDB-2345: The electron microscopy reconstruction of the tripod of lactococc... -

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Basic information

Entry
Database: EMDB / ID: EMD-2345
TitleThe electron microscopy reconstruction of the tripod of lactococcal phage Tuc2009.
Map dataReconstruction of the tripod of lactococcal phage Tuc2009
Sample
  • Sample: Tripod of lactoccocal phage Tuc2009
  • Virus: Lactococcus phage Tuc2009 (virus)
Keywordslactococcal phage / tuc2009 / tripod / electron microscopy / single-particle
Biological speciesLactococcus phage Tuc2009 (virus)
Methodsingle particle reconstruction / negative staining / Resolution: 44.0 Å
AuthorsCollins B / Bebeacua C / Mahony J / Douillard F / Veesler D / Blangy B / Cambillau C / van Sinderen D
CitationJournal: J Virol / Year: 2013
Title: Structure and functional analysis of the host recognition device of lactococcal phage tuc2009.
Authors: Barry Collins / Cecilia Bebeacua / Jennifer Mahony / Stéphanie Blangy / François P Douillard / David Veesler / Christian Cambillau / Douwe van Sinderen /
Abstract: Many phages employ a large heteropolymeric organelle located at the tip of the tail, termed the baseplate, for host recognition. Contrast electron microscopy (EM) of the lactococcal phage Tuc2009 ...Many phages employ a large heteropolymeric organelle located at the tip of the tail, termed the baseplate, for host recognition. Contrast electron microscopy (EM) of the lactococcal phage Tuc2009 baseplate and its host-binding subunits, the so-called tripods, allowed us to obtain a low-resolution structural image of this organelle. Structural comparisons between the baseplate of the related phage TP901-1 and that of Tuc2009 demonstrated that they are highly similar, except for the presence of an additional protein in the Tuc2009 baseplate (BppATuc2009), which is attached to the top of the Tuc2009 tripod structure. Recombinantly produced Tuc2009 or TP901-1 tripods were shown to bind specifically to their particular host cell surfaces and are capable of almost fully and specifically eliminating Tuc2009 or TP901-1 phage adsorption, respectively. In the case of Tuc2009, such adsorption-blocking ability was reduced in tripods that lacked BppATuc2009, indicating that this protein increases the binding specificity and/or affinity of the Tuc2009 tripod to its host receptor.
History
DepositionMar 27, 2013-
Header (metadata) releaseApr 10, 2013-
Map releaseApr 10, 2013-
UpdateJul 17, 2013-
Current statusJul 17, 2013Processing site: PDBe / Status: Released

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Structure visualization

Movie
  • Surface view with section colored by density value
  • Surface level: 1
  • Imaged by UCSF Chimera
  • Download
  • Surface view colored by cylindrical radius
  • Surface level: 1
  • Imaged by UCSF Chimera
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Movie viewer
Structure viewerEM map:
SurfViewMolmilJmol/JSmol
Supplemental images

EMD-2345.png

emd_2345.png

Downloads & links

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Map

FileDownload / File: emd_2345.map.gz / Format: CCP4 / Size: 7.8 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
AnnotationReconstruction of the tripod of lactococcal phage Tuc2009
Projections & slices

Image control

Size
Brightness
Contrast
Others
AxesZ (Sec.)Y (Row.)X (Col.)
3.53 Å/pix.
x 128 pix.
= 451.84 Å		3.53 Å/pix.
x 128 pix.
= 451.84 Å		3.53 Å/pix.
x 128 pix.
= 451.84 Å

Surface

Projections

Slices (1/3)

Slices (1/2)

Slices (2/3)

Images are generated by Spider.

Voxel sizeX=Y=Z: 3.53 Å
Density

Histogram

Histogram (log scale)
Contour LevelBy AUTHOR: 1.0 / Movie #1: 1
Minimum - Maximum-0.00450159 - 14.17819691
Average (Standard dev.)0.05103732 (±0.56207281)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin181818
Dimensions128128128
Spacing128128128
CellA=B=C: 451.84 Å
α=β=γ: 90.0 °

CCP4 map header:

modeImage stored as Reals
Å/pix. X/Y/Z3.533.533.53
M x/y/z128128128
origin x/y/z0.0000.0000.000
length x/y/z451.840451.840451.840
α/β/γ90.00090.00090.000
start NX/NY/NZ-27-15-36
NX/NY/NZ553173
MAP C/R/S123
start NC/NR/NS181818
NC/NR/NS128128128
D min/max/mean-0.00514.1780.051

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Supplemental data

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Sample components

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Entire : Tripod of lactoccocal phage Tuc2009

EntireName: Tripod of lactoccocal phage Tuc2009
Components
  • Sample: Tripod of lactoccocal phage Tuc2009
  • Virus: Lactococcus phage Tuc2009 (virus)

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Supramolecule #1000: Tripod of lactoccocal phage Tuc2009

SupramoleculeName: Tripod of lactoccocal phage Tuc2009 / type: sample / ID: 1000 / Details: The sample was monodisperse / Oligomeric state: 3 / Number unique components: 1
Molecular weightExperimental: 381 KDa / Method: SEC/MALS/RI analysis

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Supramolecule #1: Lactococcus phage Tuc2009

SupramoleculeName: Lactococcus phage Tuc2009 / type: virus / ID: 1 / NCBI-ID: 35241 / Sci species name: Lactococcus phage Tuc2009 / Virus type: OTHER / Virus isolate: SPECIES / Virus enveloped: No / Virus empty: No
Host (natural)Organism: Lactococcus lactis (lactic acid bacteria) / Strain: UC509.9 / synonym: BACTERIA(EUBACTERIA)

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Experimental details

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Structure determination

Methodnegative staining
Processingsingle particle reconstruction
Aggregation stateparticle

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Sample preparation

BufferpH: 7.4 / Details: 20 mM Tris-HCL, 10 mM MgSO4, 100 mM NaCl
StainingType: NEGATIVE
Details: Grids with adsorbed protein floated on 2% w/v uranyl acetate for 20 seconds
GridDetails: 300 mesh copper grid with thin carbon layer, glow discharged for 30 seconds
VitrificationCryogen name: NONE / Instrument: OTHER

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Electron microscopy

MicroscopeFEI TECNAI 12
Alignment procedureLegacy - Astigmatism: Objective lens astigmatism was corrected at 100,000 times magnification
DateJun 1, 2012
Image recordingCategory: CCD / Film or detector model: GENERIC CCD / Number real images: 100 / Average electron dose: 10 e/Å2 / Details: Images were collected using a 2kx2k CCD camera
Electron beamAcceleration voltage: 120 kV / Electron source: LAB6
Electron opticsCalibrated magnification: 67500 / Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Cs: 2 mm / Nominal defocus max: 1.5 µm / Nominal defocus min: 1.5 µm / Nominal magnification: 67500
Sample stageSpecimen holder: Room temperature holder / Specimen holder model: SIDE ENTRY, EUCENTRIC

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Image processing

Final reconstructionApplied symmetry - Point group: C3 (3 fold cyclic) / Algorithm: OTHER / Resolution.type: BY AUTHOR / Resolution: 44.0 Å / Resolution method: OTHER / Software - Name: EMAN2, Spider, Xmipp / Number images used: 5400

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