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- PDB-8bl4: Cryo-EM structure of a contractile injection system in Streptomyc... -

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Basic information

Entry
Database: PDB / ID: 8bl4
TitleCryo-EM structure of a contractile injection system in Streptomyces coelicolor, the sheath-tube module in extended state.
Components
  • Phage tail protein
  • Phage tail sheath family protein
KeywordsSTRUCTURAL PROTEIN / Contractile injection system
Function / homology
Function and homology information


structural molecule activity
Similarity search - Function
Phage tail sheath protein, beta-sandwich domain / Phage tail sheath protein beta-sandwich domain / Conserved hypothetical protein CHP02241 / Bacteriophage T4, Gp19, tail tube / T4-like virus tail tube protein gp19 / Tail sheath protein, subtilisin-like domain / Phage tail sheath protein subtilisin-like domain / Tail sheath protein, C-terminal domain / Phage tail sheath C-terminal domain
Similarity search - Domain/homology
Phage tail sheath family protein / Uncharacterized protein
Similarity search - Component
Biological speciesStreptomyces coelicolor A3
MethodELECTRON MICROSCOPY / helical reconstruction / cryo EM / Resolution: 3.9 Å
AuthorsCasu, B. / Sallmen, J.W. / Schlimpert, S. / Pilhofer, M.
Funding support Switzerland, European Union, United Kingdom, 3items
OrganizationGrant numberCountry
Swiss National Science Foundation679209 Switzerland
European Research Council (ERC)679209European Union
Biotechnology and Biological Sciences Research Council (BBSRC)BB/T015349/1 United Kingdom
CitationJournal: Nat Microbiol / Year: 2023
Title: Cytoplasmic contractile injection systems mediate cell death in Streptomyces.
Authors: Bastien Casu / Joseph W Sallmen / Susan Schlimpert / Martin Pilhofer /
Abstract: Contractile injection systems (CIS) are bacteriophage tail-like structures that mediate bacterial cell-cell interactions. While CIS are highly abundant across diverse bacterial phyla, representative ...Contractile injection systems (CIS) are bacteriophage tail-like structures that mediate bacterial cell-cell interactions. While CIS are highly abundant across diverse bacterial phyla, representative gene clusters in Gram-positive organisms remain poorly studied. Here we characterize a CIS in the Gram-positive multicellular model organism Streptomyces coelicolor and show that, in contrast to most other CIS, S. coelicolor CIS (CIS) mediate cell death in response to stress and impact cellular development. CIS are expressed in the cytoplasm of vegetative hyphae and are not released into the medium. Our cryo-electron microscopy structure enabled the engineering of non-contractile and fluorescently tagged CIS assemblies. Cryo-electron tomography showed that CIS contraction is linked to reduced cellular integrity. Fluorescence light microscopy furthermore revealed that functional CIS mediate cell death upon encountering different types of stress. The absence of functional CIS had an impact on hyphal differentiation and secondary metabolite production. Finally, we identified three putative effector proteins, which when absent, phenocopied other CIS mutants. Our results provide new functional insights into CIS in Gram-positive organisms and a framework for studying novel intracellular roles, including regulated cell death and life-cycle progression in multicellular bacteria.
History
DepositionNov 9, 2022Deposition site: PDBE / Processing site: PDBE
Revision 1.0Mar 15, 2023Provider: repository / Type: Initial release
Revision 1.1Mar 22, 2023Group: Database references / Category: citation / citation_author
Item: _citation.pdbx_database_id_PubMed / _citation.title / _citation_author.identifier_ORCID
Revision 1.2Apr 12, 2023Group: Database references / Category: citation
Item: _citation.journal_volume / _citation.page_first / _citation.page_last

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
V: Phage tail sheath family protein
v: Phage tail protein
P: Phage tail sheath family protein
p: Phage tail protein
J: Phage tail sheath family protein
j: Phage tail protein
D: Phage tail sheath family protein
d: Phage tail protein
W: Phage tail sheath family protein
w: Phage tail protein
Q: Phage tail sheath family protein
q: Phage tail protein
K: Phage tail sheath family protein
k: Phage tail protein
E: Phage tail sheath family protein
e: Phage tail protein
X: Phage tail sheath family protein
x: Phage tail protein
R: Phage tail sheath family protein
r: Phage tail protein
L: Phage tail sheath family protein
l: Phage tail protein
F: Phage tail sheath family protein
f: Phage tail protein
S: Phage tail sheath family protein
s: Phage tail protein
M: Phage tail sheath family protein
m: Phage tail protein
G: Phage tail sheath family protein
g: Phage tail protein
A: Phage tail sheath family protein
a: Phage tail protein
T: Phage tail sheath family protein
t: Phage tail protein
N: Phage tail sheath family protein
n: Phage tail protein
H: Phage tail sheath family protein
h: Phage tail protein
B: Phage tail sheath family protein
b: Phage tail protein
U: Phage tail sheath family protein
u: Phage tail protein
O: Phage tail sheath family protein
o: Phage tail protein
I: Phage tail sheath family protein
i: Phage tail protein
C: Phage tail sheath family protein
c: Phage tail protein


Theoretical massNumber of molelcules
Total (without water)1,775,01148
Polymers1,775,01148
Non-polymers00
Water0
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_5551

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Components

#1: Protein ...
Phage tail sheath family protein


Mass: 57465.113 Da / Num. of mol.: 24 / Mutation: Insertion 26-IEGVG / Source method: isolated from a natural source / Source: (natural) Streptomyces coelicolor A3(2) (bacteria) / References: UniProt: Q9L0N8
#2: Protein ...
Phage tail protein


Mass: 16493.668 Da / Num. of mol.: 24 / Source method: isolated from a natural source / Source: (natural) Streptomyces coelicolor A3(2) (bacteria) / References: UniProt: Q9L0N9

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Experimental details

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Experiment

ExperimentMethod: ELECTRON MICROSCOPY
EM experimentAggregation state: PARTICLE / 3D reconstruction method: helical reconstruction

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Sample preparation

ComponentName: The sheath-tube module of a contractile injection system in Streptomyces coelicolor
Type: COMPLEX / Entity ID: all / Source: NATURAL
Source (natural)Organism: Streptomyces coelicolor A3(2) (bacteria)
Buffer solutionpH: 8
SpecimenEmbedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES
VitrificationInstrument: FEI VITROBOT MARK IV / Cryogen name: ETHANE-PROPANE

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Electron microscopy imaging

Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company
MicroscopyModel: FEI TITAN KRIOS
Electron gunElectron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM
Electron lensMode: BRIGHT FIELDBright-field microscopy / Nominal defocus max: 3500 nm / Nominal defocus min: 1500 nm
Image recordingElectron dose: 60 e/Å2 / Film or detector model: GATAN K2 SUMMIT (4k x 4k)

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Processing

CTF correctionType: PHASE FLIPPING AND AMPLITUDE CORRECTION
Helical symmertyAngular rotation/subunit: 23.1 ° / Axial rise/subunit: 38.5 Å / Axial symmetry: C6
3D reconstructionResolution: 3.9 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 18822 / Symmetry type: HELICAL

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