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- PDB-10pl: Asymmetric architecture and adaptation of Treponema flagella -

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Basic information

Entry
Database: PDB / ID: 10pl
TitleAsymmetric architecture and adaptation of Treponema flagella
Components
  • (Flagellar filament outer layer protein FlaA, ...) x 4
  • (Flagellin) x 2
  • Flagellar filament outer layer protein
  • HEAT repeat domain-containing protein
KeywordsMOTOR PROTEIN / Treponema / Flagellin / Motility / Supercoil
Function / homology
Function and homology information


periplasmic flagellum / bacterial-type flagellum-dependent cell motility / outer membrane-bounded periplasmic space / structural molecule activity
Similarity search - Function
: / TP_0437 / Flagellar filament outer layer protein FlaA, Spirochaetes / Flagellar filament outer layer protein FlaA / Flagellar filament outer layer protein Flaa / Flagellin, C-terminal domain, subdomain 2 / Flagellin, C-terminal domain / Bacterial flagellin C-terminal helical region / Flagellin / Flagellin, N-terminal domain ...: / TP_0437 / Flagellar filament outer layer protein FlaA, Spirochaetes / Flagellar filament outer layer protein FlaA / Flagellar filament outer layer protein Flaa / Flagellin, C-terminal domain, subdomain 2 / Flagellin, C-terminal domain / Bacterial flagellin C-terminal helical region / Flagellin / Flagellin, N-terminal domain / Bacterial flagellin N-terminal helical region / HEAT repeats / Armadillo-like helical / Armadillo-type fold
Similarity search - Domain/homology
HEAT repeat domain-containing protein / Flagellar filament outer layer protein / TP-0437 domain-containing protein / Flagellin / Flagellar filament outer layer protein FlaA, putative / Flagellar filament outer layer protein FlaA, putative
Similarity search - Component
Biological speciesTreponema denticola ATCC 35405 (bacteria)
MethodELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.44 Å
AuthorsWang, J. / Kurniyati, K. / Guo, W. / Botting, J.M. / Sindelar, C.V. / Li, C. / Liu, J.
Funding support United States, 5items
OrganizationGrant numberCountry
National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)R01AI087946 United States
National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)R01AI132818 United States
National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)R01AI078958 United States
National Institutes of Health/National Institute of Dental and Craniofacial Research (NIH/NIDCR)R01DE023080 United States
National Institutes of Health/National Institute of Dental and Craniofacial Research (NIH/NIDCR)R01DE034063 United States
CitationJournal: Nat Commun / Year: 2026
Title: Asymmetric architecture and adaptation of Treponema flagella.
Authors: Jiaqi Wang / Kurni Kurniyati / Wangbiao Guo / Jack M Botting / Hui Wu / Charles V Sindelar / Chunhao Li / Jun Liu /
Abstract: Spirochetes exhibit a distinctive corkscrew-like motility driven by periplasmic flagella that wrap around the cell body in a supercoiled configuration, yet the structural basis of this propulsion ...Spirochetes exhibit a distinctive corkscrew-like motility driven by periplasmic flagella that wrap around the cell body in a supercoiled configuration, yet the structural basis of this propulsion remains poorly understood. Here we combine cryo-electron microscopy, cryo-electron tomography, and genetic and biochemical analyses to determine the assembly and adaptation principles of the supercoiled flagellar filament in Treponema denticola, a major periodontal pathogen. Near-atomic structures reveal a glycosylated FlaB flagellin core encased by an asymmetric sheath. The major sheath protein FlaA forms the bulk of the sheath and mechanically couples to the core through defined interfaces required for efficient motility, whereas four minor sheath proteins (FlaA1, FlaA2, FlaAP1, and FlaAP2) assemble along the concave side of the filament to accommodate intrinsic curvature. Disruption of this asymmetric core-sheath organization compromises force transmission and impairs motility, establishing coordinated asymmetric assembly as a fundamental mechanism underlying spirochetal motility.
History
DepositionJan 30, 2026Deposition site: RCSB / Processing site: RCSB
Revision 1.0Jul 1, 2026Provider: repository / Type: Initial release
Revision 1.0Jul 1, 2026Data content type: EM metadata / Data content type: EM metadata / Provider: repository / Type: Initial release
Revision 1.0Jul 1, 2026Data content type: Half map / Part number: 1 / Data content type: Half map / Provider: repository / Type: Initial release
Revision 1.0Jul 1, 2026Data content type: Half map / Part number: 2 / Data content type: Half map / Provider: repository / Type: Initial release
Revision 1.0Jul 1, 2026Data content type: Image / Data content type: Image / Provider: repository / Type: Initial release
Revision 1.0Jul 1, 2026Data content type: Primary map / Data content type: Primary map / Provider: repository / Type: Initial release
Revision 1.1Aug 19, 2026Group: Data collection / Database references / Category: citation / citation_author / em_admin
Item: _citation.journal_volume / _citation_author.identifier_ORCID / _em_admin.last_update
Revision 1.1Aug 19, 2026Data content type: EM metadata / Data content type: EM metadata / EM metadata / Group: Database references / Experimental summary / Data content type: EM metadata / EM metadata / EM metadata / Category: citation / citation_author / em_admin / Data content type: EM metadata / EM metadata / EM metadata
Item: _citation.journal_volume / _citation_author.identifier_ORCID / _em_admin.last_update

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
Ba: Flagellin
Bd: Flagellin
Bc: Flagellin
Bb: Flagellin
Bk: Flagellin
Bj: Flagellin
Bi: Flagellin
Bh: Flagellin
Bg: Flagellin
Bf: Flagellin
Be: Flagellin
F: Flagellin
A: HEAT repeat domain-containing protein
B: Flagellar filament outer layer protein FlaA, putative
C: Flagellar filament outer layer protein FlaA, putative
D: Flagellar filament outer layer protein FlaA, putative
E: Flagellar filament outer layer protein FlaA, putative
Ab: Flagellar filament outer layer protein
Ag: Flagellar filament outer layer protein
Ah: Flagellar filament outer layer protein
Af: Flagellar filament outer layer protein
Ae: Flagellar filament outer layer protein
Ad: Flagellar filament outer layer protein
Ac: Flagellar filament outer layer protein
Aa: Flagellar filament outer layer protein


Theoretical massNumber of molelcules
Total (without water)769,17325
Polymers769,17325
Non-polymers00
Water00
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1

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Components

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Protein , 4 types, 21 molecules BaBdBcBbBkBjBiBhBgBfBeFAAbAgAhAfAeAdAcAa

#1: Protein
Flagellin


Mass: 31342.555 Da / Num. of mol.: 11 / Source method: isolated from a natural source / Source: (natural) Treponema denticola ATCC 35405 (bacteria) / References: UniProt: Q73MN1
#2: Protein Flagellin


Mass: 12487.430 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Treponema denticola ATCC 35405 (bacteria) / References: UniProt: Q73MM8
#3: Protein HEAT repeat domain-containing protein


Mass: 21413.689 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Treponema denticola ATCC 35405 (bacteria) / References: UniProt: Q73K73
#8: Protein
Flagellar filament outer layer protein


Mass: 36868.539 Da / Num. of mol.: 8 / Source method: isolated from a natural source / Source: (natural) Treponema denticola ATCC 35405 (bacteria) / References: UniProt: Q73M00

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Flagellar filament outer layer protein FlaA, ... , 4 types, 4 molecules BCDE

#4: Protein Flagellar filament outer layer protein FlaA, putative


Mass: 23017.166 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Treponema denticola ATCC 35405 (bacteria) / References: UniProt: Q73MU8
#5: Protein Flagellar filament outer layer protein FlaA, putative


Mass: 23751.732 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Treponema denticola ATCC 35405 (bacteria) / References: UniProt: Q73MU9
#6: Protein Flagellar filament outer layer protein FlaA, putative


Mass: 23693.697 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Treponema denticola ATCC 35405 (bacteria) / References: UniProt: Q73MU9
#7: Protein Flagellar filament outer layer protein FlaA, putative


Mass: 25093.322 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Treponema denticola ATCC 35405 (bacteria) / References: UniProt: Q73MU8

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Details

Has protein modificationN

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Experimental details

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Experiment

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

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Sample preparation

ComponentName: Flagellar filament of Treponema denticola / Type: COMPLEX / Entity ID: all / Source: NATURAL
Source (natural)Organism: Treponema denticola ATCC 35405 (bacteria)
Buffer solutionpH: 7.4
SpecimenEmbedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES
VitrificationCryogen 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: 2200 nm / Nominal defocus min: 1600 nm / Cs: 2.7 mm
Specimen holderCryogen: NITROGEN
Image recordingElectron dose: 70 e/Å2 / Film or detector model: GATAN K3 (6k x 4k)

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Processing

EM software
IDNameVersionCategory
1cryoSPARCparticle selection
2PHENIX1.21_5207model refinement
5cryoSPARCCTF correction
13cryoSPARC3D reconstruction
CTF correctionType: PHASE FLIPPING AND AMPLITUDE CORRECTION
3D reconstructionResolution: 3.44 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 159002 / Symmetry type: POINT
RefinementHighest resolution: 3.44 Å
Stereochemistry target values: REAL-SPACE (WEIGHTED MAP SUM AT ATOM CENTERS)
Refine LS restraints
Refine-IDTypeDev idealNumber
ELECTRON MICROSCOPYf_bond_d0.00554785
ELECTRON MICROSCOPYf_angle_d1.03873862
ELECTRON MICROSCOPYf_dihedral_angle_d6.7247588
ELECTRON MICROSCOPYf_chiral_restr0.0538162
ELECTRON MICROSCOPYf_plane_restr0.0079759

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