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- PDB-9gts: Cryo-EM structure of a contractile injection system in Streptomyc... -

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Basic information

Entry
Database: PDB / ID: 9gts
TitleCryo-EM structure of a contractile injection system in Streptomyces coelicolor, the cap portion in extended state.
Components
  • Phage tail protein
  • Phage tail sheath family protein
  • Pvc16 N-terminal domain-containing protein
KeywordsSTRUCTURAL PROTEIN / Contractile injection system
Function / homology
Function and homology information


structural molecule activity
Similarity search - Function
Pvc16, N-terminal / Pvc16 N-terminal domain / Conserved hypothetical protein CHP02241 / Phage tail sheath protein, beta-sandwich domain / Phage tail sheath protein beta-sandwich domain / 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 ...Pvc16, N-terminal / Pvc16 N-terminal domain / Conserved hypothetical protein CHP02241 / Phage tail sheath protein, beta-sandwich domain / Phage tail sheath protein beta-sandwich domain / 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
Pvc16 N-terminal domain-containing protein / Phage tail sheath family protein / Phage tail protein
Similarity search - Component
Biological speciesStreptomyces coelicolor A3
MethodELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.4 Å
AuthorsCasu, B. / Sallmen, J.W. / Hass, P.E. / Afanasyev, P. / Xu, J. / Schlimpert, S. / Pilhofer, M.
Funding support Switzerland, European Union, United Kingdom, 4items
OrganizationGrant numberCountry
Swiss National Science Foundation31003A_179255 Switzerland
European Research Council (ERC)679209European Union
Biotechnology and Biological Sciences Research Council (BBSRC)BB/T015349/1 United Kingdom
Biotechnology and Biological Sciences Research Council (BBSRC)BB/X01097X/1 United Kingdom
CitationJournal: Elife / Year: 2025
Title: Function and firing of the contractile injection system requires the membrane protein CisA.
Authors: Bastien Casu / Joseph W Sallmen / Peter E Haas / Govind Chandra / Pavel Afanasyev / Jingwei Xu / Martin Pilhofer / Susan Schlimpert /
Abstract: Bacterial contractile injection systems (CIS) are phage tail-like macromolecular complexes that mediate cell-cell interactions by injecting effector proteins into target cells. CIS from (CIS) are ...Bacterial contractile injection systems (CIS) are phage tail-like macromolecular complexes that mediate cell-cell interactions by injecting effector proteins into target cells. CIS from (CIS) are localized in the cytoplasm. Under stress, they induce cell death and impact the life cycle. It remains unknown, however, whether CIS require accessory proteins to directly interact with the cytoplasmic membrane to function. Here, we characterize the putative membrane adaptor CisA, a conserved factor in CIS gene clusters across species. We show by cryo-electron tomography imaging and in vivo assays that CIS contraction and function depend on CisA. Using single-particle cryo-electron microscopy, we provide an atomic model of the extended CIS apparatus; however, CisA is not part of the complex. Instead, our findings show that CisA is a membrane protein with a cytoplasmic N-terminus predicted to interact with CIS components, thereby providing a possible mechanism for mediating CIS recruitment to the membrane and subsequent firing. Our work shows that CIS function in multicellular bacteria is distinct from type VI secretion systems and extracellular CIS, and possibly evolved due to the role CIS play in regulated cell death.
History
DepositionSep 18, 2024Deposition site: PDBE / Processing site: PDBE
Revision 1.0Jun 18, 2025Provider: repository / Type: Initial release
Revision 1.0Jun 18, 2025Data content type: EM metadata / Data content type: EM metadata / Provider: repository / Type: Initial release
Revision 1.0Jun 18, 2025Data content type: Half map / Part number: 1 / Data content type: Half map / Provider: repository / Type: Initial release
Revision 1.0Jun 18, 2025Data content type: Half map / Part number: 2 / Data content type: Half map / Provider: repository / Type: Initial release
Revision 1.0Jun 18, 2025Data content type: Image / Data content type: Image / Provider: repository / Type: Initial release
Revision 1.0Jun 18, 2025Data content type: Mask / Part number: 1 / Data content type: Mask / Provider: repository / Type: Initial release
Revision 1.0Jun 18, 2025Data content type: Primary map / Data content type: Primary map / Provider: repository / Type: Initial release
Revision 1.1Jul 16, 2025Group: Data collection / Database references / Category: citation / citation_author / em_admin
Item: _citation.country / _citation.journal_abbrev ..._citation.country / _citation.journal_abbrev / _citation.journal_id_CSD / _citation.journal_id_ISSN / _citation.journal_volume / _citation.pdbx_database_id_DOI / _citation.pdbx_database_id_PubMed / _citation.title / _citation.year / _em_admin.last_update

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
1a: Phage tail protein
1f: Phage tail protein
1e: Phage tail protein
1d: Phage tail protein
1c: Phage tail protein
1b: Phage tail protein
2A: Phage tail sheath family protein
0A: Pvc16 N-terminal domain-containing protein
2F: Phage tail sheath family protein
0F: Pvc16 N-terminal domain-containing protein
2E: Phage tail sheath family protein
0E: Pvc16 N-terminal domain-containing protein
2D: Phage tail sheath family protein
0D: Pvc16 N-terminal domain-containing protein
2C: Phage tail sheath family protein
0C: Pvc16 N-terminal domain-containing protein
2B: Phage tail sheath family protein
0B: Pvc16 N-terminal domain-containing protein


Theoretical massNumber of molelcules
Total (without water)592,03118
Polymers592,03118
Non-polymers00
Water00
1


  • Idetical with deposited unit
  • defined by author&software
  • Evidence: electron microscopy, not applicable
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1

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Components

#1: Protein
Phage tail protein


Mass: 16493.668 Da / Num. of mol.: 6 / Source method: isolated from a natural source / Source: (natural) Streptomyces coelicolor A3(2) (bacteria) / References: UniProt: Q9L0N9
#2: Protein
Phage tail sheath family protein


Mass: 57465.113 Da / Num. of mol.: 6 / Source method: isolated from a natural source / Source: (natural) Streptomyces coelicolor A3(2) (bacteria) / References: UniProt: Q9L0N8
#3: Protein
Pvc16 N-terminal domain-containing protein


Mass: 24713.115 Da / Num. of mol.: 6 / Source method: isolated from a natural source / Source: (natural) Streptomyces coelicolor A3(2) (bacteria) / References: UniProt: Q8CJU2
Has protein modificationN

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Experimental details

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Experiment

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

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Sample preparation

ComponentName: The cap 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: TFS KRIOS
Electron gunElectron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM
Electron lensMode: BRIGHT FIELD / Nominal defocus max: 3000 nm / Nominal defocus min: 1000 nm
Image recordingElectron dose: 60 e/Å2 / Film or detector model: GATAN K3 BIOQUANTUM (6k x 4k)

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Processing

CTF correctionType: PHASE FLIPPING AND AMPLITUDE CORRECTION
3D reconstructionResolution: 3.4 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 19218 / Symmetry type: POINT

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