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- EMDB-45169: Shigella flexneri bacteriophage Sf14 Tail Baseplate -

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Basic information

Entry
Database: EMDB / ID: EMD-45169
TitleShigella flexneri bacteriophage Sf14 Tail Baseplate
Map data
Sample
  • Virus: Shigella phage Sf14 (virus)
KeywordsSf14 / VIRUS
Biological speciesShigella phage Sf14 (virus)
Methodsingle particle reconstruction / cryo EM / Resolution: 4.0 Å
AuthorsSubramanian S / Kerns HR / Braverman SG / Doore SM
Funding support United States, 2 items
OrganizationGrant numberCountry
National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)R01AI170608 United States
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)U24GM116789 United States
CitationJournal: Commun Biol / Year: 2025
Title: The structure of Shigella virus Sf14 reveals the presence of two decoration proteins and two long tail fibers.
Authors: Sundharraman Subramanian / Hailey R Kerns / Samantha G Braverman / Sarah M Doore /
Abstract: Bacteriophage Sf14 infects the human pathogen Shigella flexneri. A previous low-resolution structure suggested the presence of a decoration protein on its T = 9 icosahedral capsid. Here, we ...Bacteriophage Sf14 infects the human pathogen Shigella flexneri. A previous low-resolution structure suggested the presence of a decoration protein on its T = 9 icosahedral capsid. Here, we determined high-resolution structures of the Sf14 capsid and neck, along with a moderate-resolution structure of the whole Sf14 tail and baseplate. These structures indicate the capsid has not one, but two different types of decoration proteins: a trimeric β-tulip lattice that covers the entire capsid and a set of Hoc-like proteins that bind preferentially to hexamers at the quasi-3-fold axes of symmetry. The neck also contains two sets of whiskers oriented in opposite directions, and the tail has two types of long tail fibers which may bind different receptors. Based on homology and phylogenetic analysis, Sf14 may be the product of multiple horizontal gene transfer events. The structures presented here can be used to investigate further hypotheses of phage structure-function relationships and structural diversity.
History
DepositionMay 31, 2024-
Header (metadata) releaseFeb 5, 2025-
Map releaseFeb 5, 2025-
UpdateAug 20, 2025-
Current statusAug 20, 2025Processing site: RCSB / Status: Released

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Structure visualization

Supplemental images

emd_45169.png

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Map

FileDownload / File: emd_45169.map.gz / Format: CCP4 / Size: 1.9 GB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Projections & slices

Image control

Size
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AxesZ (Sec.)Y (Row.)X (Col.)
0.82 Å/pix.
x 800 pix.
= 652.8 Å		0.82 Å/pix.
x 800 pix.
= 652.8 Å		0.82 Å/pix.
x 800 pix.
= 652.8 Å

Surface

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Images are generated by Spider.

Voxel sizeX=Y=Z: 0.816 Å
Density

Histogram

Histogram (log scale)
Contour LevelBy AUTHOR: 0.125
Minimum - Maximum-0.4872168 - 0.83845234
Average (Standard dev.)-0.000082213985 (±0.041558906)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin-400-400-400
Dimensions800800800
Spacing800800800
CellA=B=C: 652.8 Å
α=β=γ: 90.0 °

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Supplemental data

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Mask #1

Fileemd_45169_msk_1.map
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AxesZYX

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Half map: #1

Fileemd_45169_half_map_1.map
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Half map: #2

Fileemd_45169_half_map_2.map
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Sample components

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Entire : Shigella phage Sf14

EntireName: Shigella phage Sf14 (virus)
Components
  • Virus: Shigella phage Sf14 (virus)

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Supramolecule #1: Shigella phage Sf14

SupramoleculeName: Shigella phage Sf14 / type: virus / ID: 1 / Parent: 0 / Macromolecule list: #1-#16 / NCBI-ID: 2024304 / Sci species name: Shigella phage Sf14 / Virus type: VIRION / Virus isolate: OTHER / Virus enveloped: No / Virus empty: No
Host (natural)Organism: Shigella flexneri Y (bacteria)

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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
Component:
ConcentrationFormulaName
10.0 mMTristris(hydroxymethyl)aminomethane
10.0 mMMgCl2magnesium chloride
VitrificationCryogen name: ETHANE / Chamber humidity: 100 % / Chamber temperature: 277.15 K / Instrument: FEI VITROBOT MARK IV

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Electron microscopy

MicroscopeFEI TITAN KRIOS
Image recordingFilm or detector model: GATAN K3 BIOQUANTUM (6k x 4k) / Average electron dose: 33.0 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 3.5 µm / Nominal defocus min: 0.5 µm
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

CTF correctionType: NONE
Startup modelType of model: NONE
Final reconstructionResolution.type: BY AUTHOR / Resolution: 4.0 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 11474
Initial angle assignmentType: PROJECTION MATCHING / Software - Name: cryoSPARC (ver. 4.4.1)
Final angle assignmentType: PROJECTION MATCHING / Software - Name: cryoSPARC (ver. 4.4.1)
FSC plot (resolution estimation)

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