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- PDB-9myg: Cryo-EM structure of Natrinema sp. J7-2 Type IV pilus, PilA1 -

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Basic information

Entry
Database: PDB / ID: 9myg
TitleCryo-EM structure of Natrinema sp. J7-2 Type IV pilus, PilA1
ComponentsArchaeal Type IV pilin N-terminal domain-containing protein
KeywordsPROTEIN FIBRIL / Type IV pilus / Pilin / Biofilm
Function / homology:
Function and homology information
Biological speciesNatrinema sp. J7-2 (archaea)
MethodELECTRON MICROSCOPY / helical reconstruction / cryo EM / Resolution: 3.8 Å
AuthorsSonani, R.R. / Egelman, E.H.
Funding support United States, 1items
OrganizationGrant numberCountry
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)GM122510 United States
CitationJournal: Cell Rep / Year: 2025
Title: A type IV pili-mediated mutualism between two co-resident temperate archaeal viruses and their host.
Authors: Jialin Xiang / Ravi R Sonani / Yangyang Wang / Zhao Chen / Weiyan Xiong / Jiangling Chen / Shuyu Li / Kang An / Yixuan Wang / Ying Liu / Mark A B Kreutzberger / Mart Krupovic / Edward H ...Authors: Jialin Xiang / Ravi R Sonani / Yangyang Wang / Zhao Chen / Weiyan Xiong / Jiangling Chen / Shuyu Li / Kang An / Yixuan Wang / Ying Liu / Mark A B Kreutzberger / Mart Krupovic / Edward H Egelman / Shishen Du / Xiangdong Chen /
Abstract: Co-resident temperate viruses are ubiquitous in prokaryotes, which interact with each other and affect their shared host. However, how such virus-virus and virus-host interactions play out in Archaea ...Co-resident temperate viruses are ubiquitous in prokaryotes, which interact with each other and affect their shared host. However, how such virus-virus and virus-host interactions play out in Archaea remains largely unexplored. Here, we discover a tripartite mutualistic interaction among the co-existing temperate viruses SNJ1 and SNJ2 and their host, haloarchaeon Natrinema sp. J7. We find that the SNJ2 provirus encodes two type IV pilins (T4Ps), which hijack the host secretion machinery to assemble into distinct filaments on the host cell surface. The SNJ2-encoded pili are dispensable for the SNJ2 infection but serve as receptors for SNJ1. As a quid pro quo, SNJ1 enhances the replication of SNJ2. Furthermore, the viral pili are the dominant filaments on the cell surface and promote biofilm formation and motility of the host. A number of SNJ2-like proviruses harbor T4P genes, suggesting that T4P-mediated virus-virus and virus-host interactions are widespread in Haloarchaea.
History
DepositionJan 21, 2025Deposition site: RCSB / Processing site: RCSB
Revision 1.0Nov 26, 2025Provider: repository / Type: Initial release

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: Archaeal Type IV pilin N-terminal domain-containing protein


Theoretical massNumber of molelcules
Total (without water)15,6161
Polymers15,6161
Non-polymers00
Water00
1
A: Archaeal Type IV pilin N-terminal domain-containing protein
x 24


Theoretical massNumber of molelcules
Total (without water)374,78824
Polymers374,78824
Non-polymers00
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
helical symmetry operation23
2


  • Idetical with deposited unit
  • helical asymmetric unit
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
SymmetryHelical symmetry: (Circular symmetry: 1 / Dyad axis: no / N subunits divisor: 1 / Num. of operations: 24 / Rise per n subunits: 4.95 Å / Rotation per n subunits: 108.81 °)

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Components

#1: Protein Archaeal Type IV pilin N-terminal domain-containing protein


Mass: 15616.163 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Natrinema sp. J7-2 (archaea) / Gene: NJ7G_0728 / Production host: Natrinema sp. J7-2 (archaea) / References: UniProt: I7CEX0
Has protein modificationN

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Experimental details

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Experiment

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

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Sample preparation

ComponentName: Type IV pilus / Type: COMPLEX / Entity ID: all / Source: RECOMBINANT
Source (natural)Organism: Natrinema sp. J7-2 (archaea)
Source (recombinant)Organism: Natrinema sp. J7-2 (archaea)
Buffer solutionpH: 7
SpecimenEmbedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES
VitrificationCryogen name: ETHANE

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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: 2400 nm / Nominal defocus min: 1400 nm
Image recordingElectron dose: 50 e/Å2 / Film or detector model: GATAN K3 (6k x 4k)

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Processing

EM softwareName: PHENIX / Version: 1.20.1_4487: / Category: model refinement
CTF correctionType: PHASE FLIPPING AND AMPLITUDE CORRECTION
Helical symmertyAngular rotation/subunit: 108.81 ° / Axial rise/subunit: 4.95 Å / Axial symmetry: C1
3D reconstructionResolution: 3.8 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 35647 / Symmetry type: HELICAL
Refine LS restraints
Refine-IDTypeDev idealNumber
ELECTRON MICROSCOPYf_bond_d0.002959
ELECTRON MICROSCOPYf_angle_d0.5081308
ELECTRON MICROSCOPYf_dihedral_angle_d3.491137
ELECTRON MICROSCOPYf_chiral_restr0.046169
ELECTRON MICROSCOPYf_plane_restr0.001171

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