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- EMDB-20243: Mobile loops and electrostatic interactions maintain the flexible... -

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Basic information

Entry
Database: EMDB / ID: EMD-20243
TitleMobile loops and electrostatic interactions maintain the flexible lambda tail tube
Map datalambda tail tube
Sampletail tube of the lambda phage != Escherichia phage lambda

tail tube of the lambda phage

  • Virus: Escherichia phage lambda (virus)
Biological speciesEscherichia phage lambda (virus)
Methodhelical reconstruction / cryo EM / Resolution: 6.8 Å
AuthorsCampbell P / Duda RL
Funding support United States, 2 items
OrganizationGrant numberCountry
National Institutes of Health/National Human Genome Research InstituteR01 GM047795 United States
National Institutes of Health/National Human Genome Research InstituteS10 OD019995 United States
CitationJournal: J Mol Biol / Year: 2020
Title: Mobile Loops and Electrostatic Interactions Maintain the Flexible Tail Tube of Bacteriophage Lambda.
Authors: Patricia L Campbell / Robert L Duda / Jamie Nassur / James F Conway / Alexis Huet /
Abstract: The long flexible tail tube of bacteriophage lambda connects its capsid to the tail tip. On infection, a DNA ejection signal is passed from the tip, along the tube to the capsid that triggers passage ...The long flexible tail tube of bacteriophage lambda connects its capsid to the tail tip. On infection, a DNA ejection signal is passed from the tip, along the tube to the capsid that triggers passage of the DNA down the tube and into the host bacterium. The tail tube is built from repeating units of the major tail protein, gpV, which has two distinctive domains. Its N-terminal domain has the same fold as proteins that form the rigid inner tubes of contractile tail phages, such as T4, and its C-terminal domain adopt an Ig-like fold of unknown function. We determined structures of the lambda tail tube in free tails and in virions before and after DNA ejection using cryoelectron microscopy. Modeling of the density maps reveals how electrostatic interactions and a mobile loop participate in assembly and also impart flexibility to the tube while maintaining its integrity. We also demonstrate how a common protein fold produces rigid tubes in some phages but flexible tubes in others.
History
DepositionMay 23, 2019-
Header (metadata) releaseJun 19, 2019-
Map releaseNov 27, 2019-
UpdateFeb 12, 2020-
Current statusFeb 12, 2020Processing site: RCSB / Status: Released

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Structure visualization

Movie
  • Surface view with section colored by density value
  • Surface level: 0.024
  • Imaged by UCSF Chimera
  • Download
  • Surface view colored by cylindrical radius
  • Surface level: 0.024
  • Imaged by UCSF Chimera
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Movie viewer
Structure viewerEM map:
SurfViewMolmilJmol/JSmol
Supplemental images

emd_20243.png

Downloads & links

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Map

FileDownload / File: emd_20243.map.gz / Format: CCP4 / Size: 30.5 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Annotationlambda tail tube
Projections & slices

Image control

Size
Brightness
Contrast
Others
AxesZ (Sec.)Y (Row.)X (Col.)
1.15 Å/pix.
x 200 pix.
= 230. Å		1.15 Å/pix.
x 200 pix.
= 230. Å		1.15 Å/pix.
x 200 pix.
= 230. Å

Surface

Projections

Slices (1/3)

Slices (1/2)

Slices (2/3)

Images are generated by Spider.

Voxel sizeX=Y=Z: 1.15 Å
Density

Histogram

Histogram (log scale)
Contour LevelBy EMDB: 0.024 / Movie #1: 0.024
Minimum - Maximum-0.01971811 - 0.051706627
Average (Standard dev.)0.0016239218 (±0.0067057796)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions200200200
Spacing200200200
CellA=B=C: 230.0 Å
α=β=γ: 90.0 °

CCP4 map header:

modeImage stored as Reals
Å/pix. X/Y/Z1.151.151.15
M x/y/z200200200
origin x/y/z0.0000.0000.000
length x/y/z230.000230.000230.000
α/β/γ90.00090.00090.000
start NX/NY/NZ000
NX/NY/NZ360360360
MAP C/R/S123
start NC/NR/NS000
NC/NR/NS200200200
D min/max/mean-0.0200.0520.002

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Supplemental data

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Sample components

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Entire : tail tube of the lambda phage

EntireName: tail tube of the lambda phage
Components
  • Virus: Escherichia phage lambda (virus)

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Supramolecule #1: Escherichia phage lambda

SupramoleculeName: Escherichia phage lambda / type: virus / ID: 1 / Parent: 0 / Macromolecule list: #1 / Details: empty purified virus / NCBI-ID: 10710 / Sci species name: Escherichia phage lambda / Virus type: VIRION / Virus isolate: OTHER / Virus enveloped: No / Virus empty: Yes
Host (natural)Organism: Escherichia coli (E. coli)
Molecular weightTheoretical: 37 kDa/nm

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Experimental details

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Structure determination

Methodcryo EM
Processinghelical reconstruction
Aggregation stateparticle

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Sample preparation

Concentration1 mg/mL
BufferpH: 7.5
Component:
ConcentrationNameFormula
10.0 mMTris
10.0 mMmagnesium chlorideMgSO4
GridDetails: unspecified
VitrificationCryogen name: ETHANE-PROPANE / Chamber humidity: 100 % / Chamber temperature: 298 K / Instrument: FEI VITROBOT MARK II
Detailspurified virion; empty particles

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Electron microscopy

MicroscopeFEI POLARA 300
Image recordingFilm or detector model: FEI FALCON II (4k x 4k) / Detector mode: INTEGRATING / Number grids imaged: 1 / Number real images: 1500 / Average electron dose: 20.0 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD
Sample stageCooling holder cryogen: NITROGEN
Experimental equipment
Model: Tecnai Polara / Image courtesy: FEI Company

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Image processing

Final reconstructionApplied symmetry - Helical parameters - Δz: 42.8 Å
Applied symmetry - Helical parameters - Δ&Phi: 17.5 °
Applied symmetry - Helical parameters - Axial symmetry: C6 (6 fold cyclic)
Resolution.type: BY AUTHOR / Resolution: 6.8 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: RELION / Number images used: 1138
CTF correctionSoftware - Name: CTFFIND
Segment selectionNumber selected: 1504 / Software - Name: EMAN2
Final angle assignmentType: NOT APPLICABLE / Software - Name: RELION (ver. 2)
FSC plot (resolution estimation)

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Atomic model buiding 1

Initial model
PDB IDChain

2k4q

chain_id: A

2l04

chain_id: A
RefinementSpace: REAL / Protocol: FLEXIBLE FIT / Overall B value: 200

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