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- PDB-9y93: Tetrameric InvE from Salmonella Typhimurium -

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Basic information

Entry
Database: PDB / ID: 9y93
TitleTetrameric InvE from Salmonella Typhimurium
ComponentsInvasion protein InvE
KeywordsPROTEIN TRANSPORT / tetramer / gatekeeper protein / T3SS
Function / homology
Function and homology information


protein secretion by the type III secretion system / outer membrane / negative regulation of protein secretion / cell surface / plasma membrane
Similarity search - Function
Salmonella/Shigella invasion protein E / Type III secretion regulator, YopN/LcrE/InvE/MxiC / Hypersensitivity response secretion-like, HrpJ / HrpJ-like domain
Similarity search - Domain/homology
Invasion protein InvE
Similarity search - Component
Biological speciesSalmonella enterica subsp. enterica serovar Typhimurium (bacteria)
MethodELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 2.42 Å
AuthorsZhu, L.Y. / Wang, T.T. / Guo, E.Z. / Lara-Tejero, M. / Galan, J.E.
Funding support United States, 1items
OrganizationGrant numberCountry
National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)AI030492 United States
CitationJournal: Proc Natl Acad Sci U S A / Year: 2026
Title: Oligomeric assembly of the gatekeeper InvE orchestrates hierarchical type III protein secretion in Typhimurium.
Authors: Tingting Wang / Liyan Zhu / Emily Guo / Chunxiang Wu / Florian Schueder / Maria Lara-Tejero / Jorge E Galán /
Abstract: Type III secretion systems (T3SS) are critical virulence machines in many Gram-negative bacteria, enabling hierarchical secretion of translocases followed by effectors. In the serovar Typhimurium ...Type III secretion systems (T3SS) are critical virulence machines in many Gram-negative bacteria, enabling hierarchical secretion of translocases followed by effectors. In the serovar Typhimurium SPI-1 T3SS, the regulatory protein InvE (SctW) enforces this order. Here, we show that InvE assembles into tetramers and higher-order oligomers and that oligomerization is essential for function. A 2.4 Å cryo-electron microscopy (cryo-EM) structure reveals a tetramer built as a dimer of antiparallel dimers. Photocrosslinking maps one set of residues to the interdimer seams in this tetramer, while crosslinks from additional sites suggest lateral docking between dimers in alternative registries in vivo. Blue-native electrophoresis and SEC-MALS detect native high-molecular-weight species consistent with such assemblies. DNA-PAINT superresolution microscopy confirms the presence of higher-order InvE oligomers in vivo. Charge-reversal mutations that disrupt oligomerization collapse InvE to monomers and abolish secretion, effector translocation, invasion, and virulence. Together, these data define an oligomerization-based switch in which InvE reuses the dimeric face to form higher-order contacts that govern the transition from translocase to effector secretion.
History
DepositionSep 13, 2025Deposition site: RCSB / Processing site: RCSB
Revision 1.0Jan 21, 2026Provider: repository / Type: Initial release
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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Invasion protein InvE
B: Invasion protein InvE
C: Invasion protein InvE
D: Invasion protein InvE


Theoretical massNumber of molelcules
Total (without water)182,1554
Polymers182,1554
Non-polymers00
Water00
1


  • Idetical with deposited unit
  • defined by author&software
  • Evidence: electron microscopy, not applicable, light scattering, SEC-MALS were performed to measure the molecular weight of the InvE oligomer., cross-linking, DSS chemical crosslink and ...Evidence: electron microscopy, not applicable, light scattering, SEC-MALS were performed to measure the molecular weight of the InvE oligomer., cross-linking, DSS chemical crosslink and photocrosslink were performed to confirm its molecular weight in SDS-PAGE gel.
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1

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Components

#1: Protein
Invasion protein InvE


Mass: 45538.781 Da / Num. of mol.: 4
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Salmonella enterica subsp. enterica serovar Typhimurium (bacteria)
Gene: invE, STM2897 / Production host: Escherichia coli (E. coli) / References: UniProt: P35671
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: InvE / Type: COMPLEX
Details: In Salmonella enterica serovar Typhimurium, the SPI 1 gatekeeper InvE governs the hierarchical secretion of T3SS substrates. Here InvE forms a homotetramer. Its oligomeric assemblies is essential for function.
Entity ID: all / Source: RECOMBINANT
Molecular weightExperimental value: NO
Source (natural)Organism: Salmonella enterica subsp. enterica serovar Typhimurium (bacteria)
Source (recombinant)Organism: Escherichia coli (E. coli) / Strain: BL21
Buffer solutionpH: 7.4
SpecimenEmbedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES
VitrificationInstrument: FEI VITROBOT MARK III / Cryogen 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: 2200 nm / Nominal defocus min: 1200 nm
Image recordingElectron dose: 50 e/Å2 / Film or detector model: GATAN K3 BIOQUANTUM (6k x 4k)

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Processing

EM software
IDNameVersionCategoryDetails
1cryoSPARCparticle selection
2PHENIX1.21.1_5286model refinement
13cryoSPARC4.4.13D reconstructionlocal refinement job was used to generate the final map
CTF correctionType: PHASE FLIPPING AND AMPLITUDE CORRECTION
3D reconstructionResolution: 2.42 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 2169983 / Symmetry type: POINT
RefinementHighest resolution: 2.42 Å
Stereochemistry target values: REAL-SPACE (WEIGHTED MAP SUM AT ATOM CENTERS)
Refine LS restraints
Refine-IDTypeDev idealNumber
ELECTRON MICROSCOPYf_bond_d0.0039252
ELECTRON MICROSCOPYf_angle_d0.4312484
ELECTRON MICROSCOPYf_dihedral_angle_d3.3521224
ELECTRON MICROSCOPYf_chiral_restr0.0331435
ELECTRON MICROSCOPYf_plane_restr0.0031569

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