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- EMDB-39786: Cryo-EM structure of the LRR protein within the polar flagellar motor -

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Basic information

Entry
Database: EMDB / ID: EMD-39786
TitleCryo-EM structure of the LRR protein within the polar flagellar motor
Map dataMain map
Sample
  • Complex: The polar flagellar motor-hook complex
    • Protein or peptide: Leucine-rich repeat protein
    • Protein or peptide: Flagellar basal-body rod protein FlgG
    • Protein or peptide: Flagellar M-ring protein
    • Protein or peptide: Flagellar basal body rod protein FlgB
    • Protein or peptide: Flagellar basal-body rod protein FlgC
    • Protein or peptide: Flagellar basal-body rod protein FlgF
KeywordsPolar flagellum / Polar flagellar motor / LRR / MOTOR PROTEIN
Function / homology
Function and homology information


bacterial-type flagellum basal body, distal rod / bacterial-type flagellum basal body, rod / bacterial-type flagellum basal body, MS ring / bacterial-type flagellum-dependent swarming motility / cytoskeletal motor activity / bacterial-type flagellum-dependent cell motility / plasma membrane
Similarity search - Function
Flagellar basal-body rod FlgF / Flagellar basal-body rod FlgG / Flagellar basal-body rod protein FlgC / Flagellar basal-body rod protein FlgB / Flagellar hook-basal body protein, FlgE/F/G / Flagellar hook-basal body protein, FlgE/F/G-like / : / Flagellar hook protein FlgE/F/G D1 domain / Flagellar basal body rod protein, conserved site / Flagella basal body rod proteins signature. ...Flagellar basal-body rod FlgF / Flagellar basal-body rod FlgG / Flagellar basal-body rod protein FlgC / Flagellar basal-body rod protein FlgB / Flagellar hook-basal body protein, FlgE/F/G / Flagellar hook-basal body protein, FlgE/F/G-like / : / Flagellar hook protein FlgE/F/G D1 domain / Flagellar basal body rod protein, conserved site / Flagella basal body rod proteins signature. / Flagellar basal body rod protein, N-terminal / Flagellar basal-body/hook protein, C-terminal domain / Flagella basal body rod protein / Flagellar basal body rod FlgEFG protein C-terminal / Flagellar M-ring protein FliF / Flagellar M-ring C-terminal / Flagellar M-ring protein C-terminal / Lipoprotein YscJ/Flagellar M-ring protein / Secretory protein of YscJ/FliF family / Flagellar M-ring , N-terminal / AMP-binding enzyme, C-terminal domain superfamily
Similarity search - Domain/homology
Flagellar basal body rod protein FlgB / Flagellar basal-body rod protein FlgC / Flagellar basal-body rod protein FlgF / Flagellar basal-body rod protein FlgG / : / Flagellar M-ring protein
Similarity search - Component
Biological speciesVibrio alginolyticus (bacteria)
Methodsingle particle reconstruction / cryo EM / Resolution: 3.46 Å
AuthorsZhang L / Tan JX / Zhou Y / Zhu YQ
Funding support China, 3 items
OrganizationGrant numberCountry
National Natural Science Foundation of China (NSFC)81925024 China
National Natural Science Foundation of China (NSFC)U23A20163 China
Ministry of Science and Technology (MoST, China)2017YFA0503900 China
CitationJournal: To Be Published
Title: Cryo-EM structure of the LRR protein within the polar flagellar motor
Authors: Zhang L / Tan JX / Zhou Y / Zhu YQ
History
DepositionApr 18, 2024-
Header (metadata) releaseOct 22, 2025-
Map releaseOct 22, 2025-
UpdateOct 22, 2025-
Current statusOct 22, 2025Processing site: PDBj / Status: Released

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Structure visualization

Supplemental images

emd_39786.png

Downloads & links

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Map

FileDownload / File: emd_39786.map.gz / Format: CCP4 / Size: 909.2 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
AnnotationMain map
Projections & slices

Image control

Size
Brightness
Contrast
Others
AxesZ (Sec.)Y (Row.)X (Col.)
1.2 Å/pix.
x 620 pix.
= 744. Å		1.2 Å/pix.
x 620 pix.
= 744. Å		1.2 Å/pix.
x 620 pix.
= 744. Å

Surface

Projections

Slices (1/3)

Slices (1/2)

Slices (2/3)

Images are generated by Spider.

Voxel sizeX=Y=Z: 1.2 Å
Density

Histogram

Histogram (log scale)
Contour LevelBy AUTHOR: 0.3
Minimum - Maximum-1.2567863 - 2.0140498
Average (Standard dev.)-0.0018428474 (±0.07251015)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions620620620
Spacing620620620
CellA=B=C: 744.0 Å
α=β=γ: 90.0 °

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Supplemental data

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Half map: Half map A

Fileemd_39786_half_map_1.map
AnnotationHalf map A
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Half map: Half map B

Fileemd_39786_half_map_2.map
AnnotationHalf map B
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Sample components

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Entire : The polar flagellar motor-hook complex

EntireName: The polar flagellar motor-hook complex
Components
  • Complex: The polar flagellar motor-hook complex
    • Protein or peptide: Leucine-rich repeat protein
    • Protein or peptide: Flagellar basal-body rod protein FlgG
    • Protein or peptide: Flagellar M-ring protein
    • Protein or peptide: Flagellar basal body rod protein FlgB
    • Protein or peptide: Flagellar basal-body rod protein FlgC
    • Protein or peptide: Flagellar basal-body rod protein FlgF

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Supramolecule #1: The polar flagellar motor-hook complex

SupramoleculeName: The polar flagellar motor-hook complex / type: complex / ID: 1 / Parent: 0 / Macromolecule list: all
Source (natural)Organism: Vibrio alginolyticus (bacteria) / Strain: KK148

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Macromolecule #1: Leucine-rich repeat protein

MacromoleculeName: Leucine-rich repeat protein / type: protein_or_peptide / ID: 1 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Vibrio alginolyticus (bacteria) / Strain: KK148
Molecular weightTheoretical: 21.518053 KDa
SequenceString: MRFVSLFLTL MLLCFPSFAY ELDYYSKFGH TDNYGNLDLR NKPYTQLPSG FVVKGNLNIS QTPIKKLPKG LDVGGSLEAT NSALKTIRS GTKIKGYANL LGSKIESWPR GIKLGGYLNL TDTPLKTLPA KLRVKGDLSV IRTPISALPE GLVVDGNLYI G GSALQVFP ...String:
MRFVSLFLTL MLLCFPSFAY ELDYYSKFGH TDNYGNLDLR NKPYTQLPSG FVVKGNLNIS QTPIKKLPKG LDVGGSLEAT NSALKTIRS GTKIKGYANL LGSKIESWPR GIKLGGYLNL TDTPLKTLPA KLRVKGDLSV IRTPISALPE GLVVDGNLYI G GSALQVFP DTMTVKGNIF LGGNKITKWP SNLTLGGAVA P

UniProtKB: UNIPROTKB: A0A9W4FN72

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Macromolecule #2: Flagellar basal-body rod protein FlgG

MacromoleculeName: Flagellar basal-body rod protein FlgG / type: protein_or_peptide / ID: 2 / Number of copies: 6 / Enantiomer: LEVO
Source (natural)Organism: Vibrio alginolyticus (bacteria) / Strain: KK148
Molecular weightTheoretical: 27.908943 KDa
SequenceString: MHPALWVSKT GLDAQQTNIA TISNNLANAS TVGYKKSRAV FEDLFYQNIN QPGGQSSQNT ELPSGLMLGA GSKVVATQKV HTHGNAQTT TNALDMMVEG DGFFQVTLPD GNIGYTRNGQ FTLNGEGTLV TSGSGYPVEP EIVIPEDAIS ITVGTDGEVS V RVRGQQDN ...String:
MHPALWVSKT GLDAQQTNIA TISNNLANAS TVGYKKSRAV FEDLFYQNIN QPGGQSSQNT ELPSGLMLGA GSKVVATQKV HTHGNAQTT TNALDMMVEG DGFFQVTLPD GNIGYTRNGQ FTLNGEGTLV TSGSGYPVEP EIVIPEDAIS ITVGTDGEVS V RVRGQQDN QVVGQLTITD FVNPGGLEPI GQNLYLPTGA SGDPQEGVPG LDGLGEIRQS MLEASNVNVT EELVNMIEAQ RV YEMNSKV ISSVDKMMSF VNQQL

UniProtKB: Flagellar basal-body rod protein FlgG

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Macromolecule #3: Flagellar M-ring protein

MacromoleculeName: Flagellar M-ring protein / type: protein_or_peptide / ID: 3 / Number of copies: 15 / Enantiomer: LEVO
Source (natural)Organism: Vibrio alginolyticus (bacteria) / Strain: KK148
Molecular weightTheoretical: 63.915605 KDa
SequenceString: MADKSTDLTV TEGGSDGALV ASSDVDVESQ NPDLEERSAS KFDMAVGDLD LLRQVVLVLS ISICVALIVM LFFWVKEPEM RPLGAYETE ELIPVLDYLD QQKINYKLDG NTISVESSEY NSIKLGMVRS GVNQATEAGD DILLQDMGFG VSQRLEQERL K LSRERQLA ...String:
MADKSTDLTV TEGGSDGALV ASSDVDVESQ NPDLEERSAS KFDMAVGDLD LLRQVVLVLS ISICVALIVM LFFWVKEPEM RPLGAYETE ELIPVLDYLD QQKINYKLDG NTISVESSEY NSIKLGMVRS GVNQATEAGD DILLQDMGFG VSQRLEQERL K LSRERQLA QAIEEMKQVR KARVLLALPK HSVFVRHNQE ASASVFLTLS TGTNLKQQEV DSIVDMVASA VPGMKTSRIT VT DQHGRLL SSGSQDPASA ARRKEQELER SQEQALREKI DSVLLPILGY GNYTAQVDIQ MDFSAVEQTR KRFDPNTPAT RSE YALEDY NNGNMVAGIP GALSNQPPAD ASIPQDVAQM KDGSVMGQGS VRKESTRNFE LDTTISHERK QTGTVARQTV SVAI KDRRQ VNPDTGEVTY TPMSESEINA IRQVLIGTVG FDQGRGDLLN VLSVKFAEPE AEQLEEPPIW EHPNFSDWVR WFASA LVII VVVLVLVRPA MKKLLNPTSD DEDEMYGPDG LPIGADGETS LIGSDIESSE LFEFGSSIDL PNLHKDEDVL KAVRAL VAN EPELAAQVVK NWMNDNG

UniProtKB: Flagellar M-ring protein

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Macromolecule #4: Flagellar basal body rod protein FlgB

MacromoleculeName: Flagellar basal body rod protein FlgB / type: protein_or_peptide / ID: 4 / Number of copies: 5 / Enantiomer: LEVO
Source (natural)Organism: Vibrio alginolyticus (bacteria) / Strain: KK148
Molecular weightTheoretical: 14.23995 KDa
SequenceString:
MAISFDNALG IHQHTVGVRE RNAEVISTNI AQANTPGYKA RGLDFAKELQ AATSGASIGL SRTDGRHIPA TTTLVGDKLY RLPTQPDTG DGNTVDLDLE RNLFMQNQIR HQASLDFLGS KFKNLTKAIK GE

UniProtKB: Flagellar basal body rod protein FlgB

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Macromolecule #5: Flagellar basal-body rod protein FlgC

MacromoleculeName: Flagellar basal-body rod protein FlgC / type: protein_or_peptide / ID: 5 / Number of copies: 6 / Enantiomer: LEVO
Source (natural)Organism: Vibrio alginolyticus (bacteria) / Strain: KK148
Molecular weightTheoretical: 14.812569 KDa
SequenceString:
MSLFNVFNVT GSAMSAESVR LNTTSSNLAN ADSVSSSAKD TYKARHAVFG AELSNAMRGG DTVPVKVMGI VESDKPLSAE YNPDHPLAN EEGYIYKPNV NVMEEMANMI SASRAYQTNV QVADSSKQML LRTLQMGQ

UniProtKB: Flagellar basal-body rod protein FlgC

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Macromolecule #6: Flagellar basal-body rod protein FlgF

MacromoleculeName: Flagellar basal-body rod protein FlgF / type: protein_or_peptide / ID: 6 / Number of copies: 5 / Enantiomer: LEVO
Source (natural)Organism: Vibrio alginolyticus (bacteria) / Strain: KK148
Molecular weightTheoretical: 26.987387 KDa
SequenceString: MDRALFLAMS GAKQNMQALQ LRANNLANVS TTGFRADLAQ ARSMQAYGEG HPSRVFSMTE RPGHNFAQGS VITTGRDLDV TIEGSGWIS VLDHTGKEGL TRNGNLKVDQ NGMLTNASGH LVLGENDAPI TLPIPLSKIE IGRDGTISVL PQGAPAEEFQ A VDRIKLVK ...String:
MDRALFLAMS GAKQNMQALQ LRANNLANVS TTGFRADLAQ ARSMQAYGEG HPSRVFSMTE RPGHNFAQGS VITTGRDLDV TIEGSGWIS VLDHTGKEGL TRNGNLKVDQ NGMLTNASGH LVLGENDAPI TLPIPLSKIE IGRDGTISVL PQGAPAEEFQ A VDRIKLVK PNDQSLFKDT NGLFRHKTPN QPYEADATVS LQTGAIEGSN VNAVGEMTAL IDLQRQFEMQ VKMMSTAEEM DK SSDSLLR MS

UniProtKB: Flagellar basal-body rod protein FlgF

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Experimental details

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Structure determination

Methodcryo EM
Processingsingle particle reconstruction
Aggregation stateparticle

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Sample preparation

BufferpH: 8
GridModel: Quantifoil R1.2/1.3 / Material: COPPER / Mesh: 300 / Support film - Material: CARBON / Support film - topology: CONTINUOUS / Support film - Film thickness: 200 / Pretreatment - Type: GLOW DISCHARGE / Pretreatment - Time: 10 sec.
VitrificationCryogen name: ETHANE / Chamber humidity: 100 % / Chamber temperature: 277.15 K / Instrument: FEI VITROBOT MARK IV

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Electron microscopy

MicroscopeFEI TITAN KRIOS
Specialist opticsEnergy filter - Name: TFS Selectris / Energy filter - Slit width: 10 eV
SoftwareName: EPU
Image recordingFilm or detector model: FEI FALCON IV (4k x 4k) / Average electron dose: 50.0 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 1.8 µm / Nominal defocus min: 1.2 µm / Nominal magnification: 105000
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

Particle selectionNumber selected: 329955
CTF correctionSoftware - Name: cryoSPARC / Type: PHASE FLIPPING AND AMPLITUDE CORRECTION
Startup modelType of model: NONE
Final reconstructionApplied symmetry - Point group: C1 (asymmetric) / Resolution.type: BY AUTHOR / Resolution: 3.46 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: cryoSPARC / Number images used: 19450
Initial angle assignmentType: MAXIMUM LIKELIHOOD / Software - Name: cryoSPARC
Final angle assignmentType: MAXIMUM LIKELIHOOD / Software - Name: cryoSPARC
FSC plot (resolution estimation)

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Atomic model buiding 1

Initial modelChain - Source name: Other / Chain - Initial model type: in silico model / Details: ModelAngelo
SoftwareName: Coot
RefinementSpace: REAL / Protocol: FLEXIBLE FIT
Output model

PDB-8z5w:
Cryo-EM structure of the LRR protein within the polar flagellar motor

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