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- PDB-10lk: Native flagellar filament from Leptospira interrogans -

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Basic information

Entry
Database: PDB / ID: 10lk
TitleNative flagellar filament from Leptospira interrogans
Components
  • (Flagellar Coiling Protein ...) x 2
  • (Flagellar filament sheath ...) x 2
  • DUF4468 domain-containing protein
  • FlaA2 associated protein 2
  • FlaA2-associated protein 1 (FlaAP)
  • Flagellin
  • HEAT repeat domain-containing protein
  • Lipoprotein
KeywordsPROTEIN FIBRIL / Bacterial Endo-flagellum / Filament
Function / homology
Function and homology information


: / : / : / : / : / Uncharacterized protein / : / : / : / :
Similarity search - Component
Biological speciesLeptospira interrogans serovar Copenhageni (bacteria)
MethodELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 4.4 Å
AuthorsBrady, M.R. / San Martin, F. / Sindelar, C.V. / Buschiazzo, A.
Funding supportUruguay, 1items
OrganizationGrant numberCountry
Agencia Nacional de Investigacion e Innovacion (ANII)Uruguay
CitationJournal: Nat Commun / Year: 2026
Title: Core-sheath coupling controls flagellar curvature and motility in Leptospira.
Authors: Fabiana San Martin / Megan R Brady / Lenka Fule / Lucienne Nouchikian / Azalia Rodriguez / Magalie Duchateau / Sonia Mondino / Nicole Larrieux / Elsio A Wunder / Albert I Ko / Martial Rey / ...Authors: Fabiana San Martin / Megan R Brady / Lenka Fule / Lucienne Nouchikian / Azalia Rodriguez / Magalie Duchateau / Sonia Mondino / Nicole Larrieux / Elsio A Wunder / Albert I Ko / Martial Rey / Julia Chamot-Rooke / Rosario Duran / Felipe Trajtenberg / Mathieu Picardeau / Charles V Sindelar / Alejandro Buschiazzo /
Abstract: Spirochaete pathogens are among the most invasive bacteria known, causing syphilis, Lyme disease, and leptospirosis. Their tissue penetration depends on periplasmic flagellar filaments that, unlike ...Spirochaete pathogens are among the most invasive bacteria known, causing syphilis, Lyme disease, and leptospirosis. Their tissue penetration depends on periplasmic flagellar filaments that, unlike other bacterial flagella, are encased in a spirochaete-specific multi-protein sheath and deform the cell body into motile waves. How these filaments achieve the mechanical properties needed for invasive motility has remained unclear. Here we determine complete atomic structures of the Leptospira endoflagellar filament, revealing an elaborate sheath of 9 to 12 distinct asymmetrically arranged proteins. We show that the flagellin variant forming the filament core determines sheath composition, producing curvatures ranging from ~3.5 µm to ~5.6 µm. The lower-curvature architecture, employed by pathogenic Leptospira interrogans, proves essential for motility in viscous environments and during infection. Thus, Leptospira achieves environment-specific motility through modular core-sheath coupling, linking atomic-scale structural plasticity to large-scale changes in swimming behaviour. Conservation of key sheath components suggests this mechanism may extend across spirochaetes.
History
DepositionJan 26, 2026Deposition site: RCSB / Processing site: RCSB
Revision 1.0Sep 2, 2026Provider: repository / Type: Initial release
Revision 1.0Sep 2, 2026Data content type: EM metadata / Data content type: EM metadata / Provider: repository / Type: Initial release

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A4: Flagellin
A5: Flagellin
A6: Flagellin
A7: Flagellin
A8: Flagellin
A9: Flagellin
B3: Flagellin
B4: Flagellin
B5: Flagellin
B6: Flagellin
B7: Flagellin
B8: Flagellin
C3: Flagellin
C4: Flagellin
C5: Flagellin
C6: Flagellin
C7: Flagellin
C8: Flagellin
D3: Flagellin
D4: Flagellin
D5: Flagellin
D6: Flagellin
D7: Flagellin
E2: Flagellin
E3: Flagellin
E4: Flagellin
E5: Flagellin
E6: Flagellin
E7: Flagellin
F2: Flagellin
F3: Flagellin
F4: Flagellin
F5: Flagellin
F6: Flagellin
G1: Flagellin
G2: Flagellin
G6: Flagellin
G7: Flagellin
G8: Flagellin
G9: Flagellin
H6: Flagellin
H7: Flagellin
H8: Flagellin
H9: Flagellin
I5: Flagellin
I6: Flagellin
I7: Flagellin
I8: Flagellin
I9: Flagellin
J5: Flagellin
J6: Flagellin
J7: Flagellin
J8: Flagellin
J9: Flagellin
K4: Flagellin
K5: Flagellin
K6: Flagellin
K7: Flagellin
K8: Flagellin
K9: Flagellin
L2: Flagellar Coiling Protein A (FcpA)
L3: Flagellar Coiling Protein A (FcpA)
L4: Flagellar Coiling Protein A (FcpA)
L5: Flagellar Coiling Protein A (FcpA)
L6: Flagellar Coiling Protein A (FcpA)
M1: Flagellar Coiling Protein A (FcpA)
M2: Flagellar Coiling Protein A (FcpA)
M3: Flagellar Coiling Protein A (FcpA)
M4: Flagellar Coiling Protein A (FcpA)
M5: Flagellar Coiling Protein A (FcpA)
N2: Flagellar Coiling Protein A (FcpA)
N3: Flagellar Coiling Protein A (FcpA)
N4: Flagellar Coiling Protein A (FcpA)
N5: Flagellar Coiling Protein A (FcpA)
N6: Flagellar Coiling Protein A (FcpA)
O1: Flagellar Coiling Protein A (FcpA)
O2: Flagellar Coiling Protein A (FcpA)
O3: Flagellar Coiling Protein A (FcpA)
O4: Flagellar Coiling Protein A (FcpA)
O5: Flagellar Coiling Protein A (FcpA)
P2: Flagellar Coiling Protein A (FcpA)
P3: Flagellar Coiling Protein A (FcpA)
P4: Flagellar Coiling Protein A (FcpA)
P5: Flagellar Coiling Protein A (FcpA)
P6: Flagellar Coiling Protein A (FcpA)
Q1: Flagellar Coiling Protein B (FcpB)
Q2: Flagellar Coiling Protein B (FcpB)
Q3: Flagellar Coiling Protein B (FcpB)
Q4: Flagellar Coiling Protein B (FcpB)
R2: Flagellar Coiling Protein B (FcpB)
R3: Flagellar Coiling Protein B (FcpB)
R4: Flagellar Coiling Protein B (FcpB)
R5: Flagellar Coiling Protein B (FcpB)
S2: Flagellar Coiling Protein B (FcpB)
S3: Flagellar Coiling Protein B (FcpB)
S4: Flagellar Coiling Protein B (FcpB)
S5: Flagellar Coiling Protein B (FcpB)
S6: Flagellar Coiling Protein B (FcpB)
T1: Flagellar filament sheath protein
T2: Flagellar filament sheath protein
T3: Flagellar filament sheath protein
T4: Flagellar filament sheath protein
V1: Flagellar filament sheath protein
V2: Flagellar filament sheath protein
V3: Flagellar filament sheath protein
V4: Flagellar filament sheath protein
V5: Flagellar filament sheath protein
X1: Flagellar filament sheath protein
X2: Flagellar filament sheath protein
X3: Flagellar filament sheath protein
X4: Flagellar filament sheath protein
X5: Flagellar filament sheath protein
Y1: FlaA2 associated protein 2
Y2: FlaA2 associated protein 2
Y3: FlaA2 associated protein 2
Y4: FlaA2 associated protein 2
Y5: FlaA2 associated protein 2
Z1: FlaA2-associated protein 1 (FlaAP)
Z2: FlaA2-associated protein 1 (FlaAP)
Z3: FlaA2-associated protein 1 (FlaAP)
Z4: FlaA2-associated protein 1 (FlaAP)
a2: DUF4468 domain-containing protein
a3: DUF4468 domain-containing protein
a4: DUF4468 domain-containing protein
a5: DUF4468 domain-containing protein
c1: Lipoprotein
c2: Lipoprotein
c3: Lipoprotein
d2: HEAT repeat domain-containing protein
d3: HEAT repeat domain-containing protein
d4: HEAT repeat domain-containing protein
h0: Flagellin
h1: Flagellin
i0: Flagellin
j0: Flagellin
p2: Flagellar Coiling Protein A (FcpA)
p3: Flagellar Coiling Protein A (FcpA)
p4: Flagellar Coiling Protein A (FcpA)
p5: Flagellar Coiling Protein A (FcpA)
s3: Flagellar Coiling Protein B (FcpB)
s4: Flagellar Coiling Protein B (FcpB)
s5: Flagellar Coiling Protein B (FcpB)
s6: Flagellar Coiling Protein B (FcpB)
t1: Flagellar filament sheath protein
t2: Flagellar filament sheath protein
t3: Flagellar filament sheath protein
t4: Flagellar filament sheath protein
hetero molecules


Theoretical massNumber of molelcules
Total (without water)4,754,413165
Polymers4,753,692147
Non-polymers72118
Water64936
1


  • Idetical with deposited unit
  • defined by author
  • Evidence: electron microscopy, not applicable
TypeNameSymmetry operationNumber
identity operation1_5551

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Components

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Protein , 6 types, 83 molecules A4A5A6A7A8A9B3B4B5B6B7B8C3C4C5C6C7C8D3D4D5D6D7E2E3E4E5E6E7F2...

#1: Protein ...
Flagellin


Mass: 31341.467 Da / Num. of mol.: 64 / Source method: isolated from a natural source / Details: part of the native flagellar filament assembly
Source: (natural) Leptospira interrogans serovar Copenhageni (bacteria)
Strain: Fiocruz L1-130 / References: UniProt: Q72R58
#6: Protein
FlaA2 associated protein 2


Mass: 33009.527 Da / Num. of mol.: 5 / Source method: isolated from a natural source
Source: (natural) Leptospira interrogans serovar Copenhageni (bacteria)
References: UniProt: A0AAV9FRP0
#7: Protein
FlaA2-associated protein 1 (FlaAP)


Mass: 43318.246 Da / Num. of mol.: 4 / Source method: isolated from a natural source
Source: (natural) Leptospira interrogans serovar Copenhageni (bacteria)
References: UniProt: Q72SU9
#8: Protein
DUF4468 domain-containing protein


Mass: 27492.506 Da / Num. of mol.: 4 / Source method: isolated from a natural source
Source: (natural) Leptospira interrogans serovar Copenhageni (bacteria)
References: UniProt: Q72NA0
#9: Protein Lipoprotein


Mass: 17128.670 Da / Num. of mol.: 3 / Source method: isolated from a natural source
Source: (natural) Leptospira interrogans serovar Copenhageni (bacteria)
References: UniProt: Q72RW3
#10: Protein HEAT repeat domain-containing protein


Mass: 33181.207 Da / Num. of mol.: 3 / Source method: isolated from a natural source
Source: (natural) Leptospira interrogans serovar Copenhageni (bacteria)
References: UniProt: Q72MR9

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Flagellar Coiling Protein ... , 2 types, 46 molecules L2L3L4L5L6M1M2M3M4M5N2N3N4N5N6O1O2O3O4O5P2P3P4P5P6p2p3p4p5Q1...

#2: Protein ...
Flagellar Coiling Protein A (FcpA)


Mass: 36270.336 Da / Num. of mol.: 29 / Source method: isolated from a natural source / Details: Part or the native flagellar filament assembly
Source: (natural) Leptospira interrogans serovar Copenhageni (bacteria)
Strain: Fiocruz L1-130 / References: UniProt: Q72MM7
#3: Protein
Flagellar Coiling Protein B (FcpB)


Mass: 32067.277 Da / Num. of mol.: 17 / Source method: isolated from a natural source / Details: Part of the native flagellar filament assembly
Source: (natural) Leptospira interrogans serovar Copenhageni (bacteria)
Strain: Fiocruz L1-130 / References: UniProt: Q72RA0

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Flagellar filament sheath ... , 2 types, 18 molecules T1T2T3T4t1t2t3t4V1V2V3V4V5X1X2X3X4X5

#4: Protein
Flagellar filament sheath protein


Mass: 34930.551 Da / Num. of mol.: 8 / Source method: isolated from a natural source / Details: Part of the native flagellar filament assembly
Source: (natural) Leptospira interrogans serovar Copenhageni (bacteria)
Strain: Fiocruz L1-130 / References: UniProt: Q72U74
#5: Protein
Flagellar filament sheath protein


Mass: 27218.984 Da / Num. of mol.: 10 / Source method: isolated from a natural source / Details: Part of the native flagellar filament assembly
Source: (natural) Leptospira interrogans serovar Copenhageni (bacteria)
Strain: Fiocruz L1-130 / References: UniProt: Q72U75

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Non-polymers , 2 types, 54 molecules

#11: Chemical
ChemComp-CA / CALCIUM ION


Mass: 40.078 Da / Num. of mol.: 18 / Source method: obtained synthetically / Formula: Ca / Feature type: SUBJECT OF INVESTIGATION
#12: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 36 / Source method: isolated from a natural source / Formula: H2O

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Details

Has ligand of interestY
Has protein modificationY

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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: Native flagellar filament / Type: COMPLEX / Entity ID: #1-#10 / Source: NATURAL
Molecular weightExperimental value: NO
Source (natural)Organism: Leptospira interrogans serovar Copenhageni (bacteria)
Strain: Fiocruz L1-130
Buffer solutionpH: 7.6
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: 3000 nm / Nominal defocus min: 1500 nm
Image recordingElectron dose: 61.5 e/Å2 / Film or detector model: GATAN K3 (6k x 4k)

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Processing

EM software
IDNameVersionCategoryDetails (eV)
1cryoSPARCparticle selectionFilament Tracer
7Coot1.1.19model fitting
8UCSF ChimeraX1.10.1model fitting
13cryoSPARC4.2.13D reconstruction
14PHENIX2.0_5936model refinement
15Servalcat0.4.128model refinement
CTF correctionType: PHASE FLIPPING AND AMPLITUDE CORRECTION
3D reconstructionResolution: 4.4 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 35760
Details: Further Density Modification with Phenix Resolve increased resolution to 4.2 angstroems and better resolved features in the cryoEM map
Symmetry type: POINT
Atomic model buildingProtocol: FLEXIBLE FIT / Space: RECIPROCAL / Target criteria: Cross-correlation coefficient
Details: Refinement iterated between real space (phenix.real_space_refine) and reciprocal space (Servalcat)
Atomic model buildingDetails: we used comparative proteomics (wt and mutants) plus cross-linked+MS data; AlphaFold-redicted Initial models; and crystallographic structures
Source name: Other / Type: integrative model

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