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- EMDB-38547: Cryo-EM structure of the protomers of the C ring in the CW state -

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Basic information

Entry
Database: EMDB / ID: EMD-38547
TitleCryo-EM structure of the protomers of the C ring in the CW state
Map dataExperimental map
Sample
  • Complex: C ring-containing flagellar motor-hook complex in the CW state
    • Complex: Constitutively active mutant of CheY
      • Protein or peptide: Chemotaxis protein CheY
    • Cell: C ring-containing flagellar motor-hook
      • Protein or peptide: Flagellar motor switch protein FliN
      • Protein or peptide: Flagellar M-ring protein
      • Protein or peptide: Flagellar motor switch protein FliM
      • Protein or peptide: Flagellar motor switch protein FliG
KeywordsFlagellum / Flagellar motor / C ring / CheY / MOTOR PROTEIN
Function / homology
Function and homology information


archaeal or bacterial-type flagellum-dependent cell motility / bacterial-type flagellum basal body, MS ring / bacterial-type flagellum basal body / bacterial-type flagellum-dependent swarming motility / positive chemotaxis / phosphorelay signal transduction system / cytoskeletal motor activity / bacterial-type flagellum-dependent cell motility / chemotaxis / metal ion binding ...archaeal or bacterial-type flagellum-dependent cell motility / bacterial-type flagellum basal body, MS ring / bacterial-type flagellum basal body / bacterial-type flagellum-dependent swarming motility / positive chemotaxis / phosphorelay signal transduction system / cytoskeletal motor activity / bacterial-type flagellum-dependent cell motility / chemotaxis / metal ion binding / plasma membrane / cytoplasm
Similarity search - Function
Flagellar motor switch protein FliN, N-terminal / Flagellar motor switch protein FliN N-terminal / : / Flagellar motor switch FliN / Flagellar motor switch FliN/Type III secretion HrcQb / Flagellar motor switch protein FliM / Flagellar motor switch protein FliM / Flagellar motor switch protein FliG / Flagellar motor switch protein FliG, alpha-helical / Flagellar motor switch protein FliG, C-terminal ...Flagellar motor switch protein FliN, N-terminal / Flagellar motor switch protein FliN N-terminal / : / Flagellar motor switch FliN / Flagellar motor switch FliN/Type III secretion HrcQb / Flagellar motor switch protein FliM / Flagellar motor switch protein FliM / Flagellar motor switch protein FliG / Flagellar motor switch protein FliG, alpha-helical / Flagellar motor switch protein FliG, C-terminal / Flagellar motor switch protein FliG, N-terminal domain / Flagellar motor switch protein FliG, middle domain / FliG C-terminal domain / FliG middle domain / FliG N-terminal domain / CheC-like superfamily / Flagellar motor switch protein FliN-like, C-terminal domain / SpoA-like superfamily / Type III flagellar switch regulator (C-ring) FliN C-term / 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 / Response regulator receiver domain / cheY-homologous receiver domain / Signal transduction response regulator, receiver domain / Response regulatory domain profile. / CheY-like superfamily
Similarity search - Domain/homology
Flagellar motor switch protein FliG / Chemotaxis protein CheY / Flagellar M-ring protein / Flagellar motor switch protein FliM / Flagellar motor switch protein FliN
Similarity search - Component
Biological speciesSalmonella enterica subsp. enterica serovar Typhimurium str. LT2 (bacteria)
Methodsingle particle reconstruction / cryo EM / Resolution: 4.4 Å
AuthorsTan JX / Zhang L / 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 protomers of the C ring in the CW state
Authors: Tan JX / Zhang L / Zhou Y / Zhu YQ
History
DepositionJan 2, 2024-
Header (metadata) releaseSep 4, 2024-
Map releaseSep 4, 2024-
UpdateSep 4, 2024-
Current statusSep 4, 2024Processing site: PDBj / Status: Released

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Structure visualization

Supplemental images

emd_38547.png

Downloads & links

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Map

FileDownload / File: emd_38547.map.gz / Format: CCP4 / Size: 824 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
AnnotationExperimental map
Projections & slices

Image control

Size
Brightness
Contrast
Others
AxesZ (Sec.)Y (Row.)X (Col.)
1.2 Å/pix.
x 600 pix.
= 720. Å		1.2 Å/pix.
x 600 pix.
= 720. Å		1.2 Å/pix.
x 600 pix.
= 720. 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: 0.15
Minimum - Maximum-0.4328578 - 0.88720435
Average (Standard dev.)-0.00046680827 (±0.018115923)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions600600600
Spacing600600600
CellA=B=C: 720.0 Å
α=β=γ: 90.0 °

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Supplemental data

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Additional map: DeepEMhancer sharpened map

Fileemd_38547_additional_1.map
AnnotationDeepEMhancer sharpened map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Half map: Half map A

Fileemd_38547_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_38547_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 : C ring-containing flagellar motor-hook complex in the CW state

EntireName: C ring-containing flagellar motor-hook complex in the CW state
Components
  • Complex: C ring-containing flagellar motor-hook complex in the CW state
    • Complex: Constitutively active mutant of CheY
      • Protein or peptide: Chemotaxis protein CheY
    • Cell: C ring-containing flagellar motor-hook
      • Protein or peptide: Flagellar motor switch protein FliN
      • Protein or peptide: Flagellar M-ring protein
      • Protein or peptide: Flagellar motor switch protein FliM
      • Protein or peptide: Flagellar motor switch protein FliG

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Supramolecule #1: C ring-containing flagellar motor-hook complex in the CW state

SupramoleculeName: C ring-containing flagellar motor-hook complex in the CW state
type: complex / ID: 1 / Parent: 0 / Macromolecule list: all
Source (natural)Organism: Salmonella enterica subsp. enterica serovar Typhimurium str. LT2 (bacteria)

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Supramolecule #2: Constitutively active mutant of CheY

SupramoleculeName: Constitutively active mutant of CheY / type: complex / ID: 2 / Parent: 1 / Macromolecule list: #5
Source (natural)Organism: Salmonella enterica subsp. enterica serovar Typhimurium str. LT2 (bacteria)

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Supramolecule #3: C ring-containing flagellar motor-hook

SupramoleculeName: C ring-containing flagellar motor-hook / type: cell / ID: 3 / Parent: 1 / Macromolecule list: #1-#4

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Macromolecule #1: Flagellar motor switch protein FliN

MacromoleculeName: Flagellar motor switch protein FliN / type: protein_or_peptide / ID: 1 / Number of copies: 9 / Enantiomer: LEVO
Source (natural)Organism: Salmonella enterica subsp. enterica serovar Typhimurium str. LT2 (bacteria)
Molecular weightTheoretical: 14.801823 KDa
SequenceString:
MSDMNNPSDE NTGALDDLWA DALNEQKATT TKSAADAVFQ QLGGGDVSGA MQDIDLIMDI PVKLTVELGR TRMTIKELLR LTQGSVVAL DGLAGEPLDI LINGYLIAQG EVVVVADKYG VRITDIITPS ERMRRLSR

UniProtKB: Flagellar motor switch protein FliN

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Macromolecule #2: Flagellar M-ring protein

MacromoleculeName: Flagellar M-ring protein / type: protein_or_peptide / ID: 2 / Number of copies: 3 / Enantiomer: LEVO
Source (natural)Organism: Salmonella enterica subsp. enterica serovar Typhimurium str. LT2 (bacteria)
Molecular weightTheoretical: 61.295645 KDa
SequenceString: MSATASTATQ PKPLEWLNRL RANPRIPLIV AGSAAVAIVV AMVLWAKTPD YRTLFSNLSD QDGGAIVAQL TQMNIPYRFA NGSGAIEVP ADKVHELRLR LAQQGLPKGG AVGFELLDQE KFGISQFSEQ VNYQRALEGE LARTIETLGP VKSARVHLAM P KPSLFVRE ...String:
MSATASTATQ PKPLEWLNRL RANPRIPLIV AGSAAVAIVV AMVLWAKTPD YRTLFSNLSD QDGGAIVAQL TQMNIPYRFA NGSGAIEVP ADKVHELRLR LAQQGLPKGG AVGFELLDQE KFGISQFSEQ VNYQRALEGE LARTIETLGP VKSARVHLAM P KPSLFVRE QKSPSASVTV TLEPGRALDE GQISAVVHLV SSAVAGLPPG NVTLVDQSGH LLTQSNTSGR DLNDAQLKFA ND VESRIQR RIEAILSPIV GNGNVHAQVT AQLDFANKEQ TEEHYSPNGD ASKATLRSRQ LNISEQVGAG YPGGVPGALS NQP APPNEA PIATPPTNQQ NAQNTPQTST STNSNSAGPR STQRNETSNY EVDRTIRHTK MNVGDIERLS VAVVVNYKTL ADGK PLPLT ADQMKQIEDL TREAMGFSDK RGDTLNVVNS PFSAVDNTGG ELPFWQQQSF IDQLLAAGRW LLVLVVAWIL WRKAV RPQL TRRVEEAKAA QEQAQVRQET EEAVEVRLSK DEQLQQRRAN QRLGAEVMSQ RIREMSDNDP RVVALVIRQW MSNDHE

UniProtKB: Flagellar M-ring protein

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Macromolecule #3: Flagellar motor switch protein FliM

MacromoleculeName: Flagellar motor switch protein FliM / type: protein_or_peptide / ID: 3 / Number of copies: 3 / Enantiomer: LEVO
Source (natural)Organism: Salmonella enterica subsp. enterica serovar Typhimurium str. LT2 (bacteria)
Molecular weightTheoretical: 37.901066 KDa
SequenceString: MGDSILSQAE IDALLNGDSD TKDEPTPGIA SDSDIRPYDP NTQRRVVRER LQALEIINER FARQFRMGLF NLLRRSPDIT VGAIRIQPY HEFARNLPVP TNLNLIHLKP LRGTGLVVFS PSLVFIAVDN LFGGDGRFPT KVEGREFTHT EQRVINRMLK L ALEGYSDA ...String:
MGDSILSQAE IDALLNGDSD TKDEPTPGIA SDSDIRPYDP NTQRRVVRER LQALEIINER FARQFRMGLF NLLRRSPDIT VGAIRIQPY HEFARNLPVP TNLNLIHLKP LRGTGLVVFS PSLVFIAVDN LFGGDGRFPT KVEGREFTHT EQRVINRMLK L ALEGYSDA WKAINPLEVE YVRSEMQVKF TNITTSPNDI VVNTPFHVEI GNLTGEFNIC LPFSMIEPLR ELLVNPPLEN SR HEDQNWR DNLVRQVQHS ELELVANFAD IPLRLSQILK LKPGDVLPIE KPDRIIAHVD GVPVLTSQYG TVNGQYALRV EHL INPILN SLNEEQPK

UniProtKB: Flagellar motor switch protein FliM

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Macromolecule #4: Flagellar motor switch protein FliG

MacromoleculeName: Flagellar motor switch protein FliG / type: protein_or_peptide / ID: 4 / Number of copies: 3 / Enantiomer: LEVO
Source (natural)Organism: Salmonella enterica subsp. enterica serovar Typhimurium str. LT2 (bacteria)
Molecular weightTheoretical: 36.890957 KDa
SequenceString: MSNLSGTDKS VILLMTIGED RAAEVFKHLS TREVQALSTA MANVRQISNK QLTDVLSEFE QEAEQFAALN INANEYLRSV LVKALGEER ASSLLEDILE TRDTTSGIET LNFMEPQSAA DLIRDEHPQI IATILVHLKR SQAADILALF DERLRHDVML R IATFGGVQ ...String:
MSNLSGTDKS VILLMTIGED RAAEVFKHLS TREVQALSTA MANVRQISNK QLTDVLSEFE QEAEQFAALN INANEYLRSV LVKALGEER ASSLLEDILE TRDTTSGIET LNFMEPQSAA DLIRDEHPQI IATILVHLKR SQAADILALF DERLRHDVML R IATFGGVQ PAALAELTEV LNGLLDGQNL KRSKMGGVRT AAEIINLMKT QQEEAVITAV REFDGELAQK IIDEMFLFEN LV DVDDRSI QRLLQEVDSE SLLIALKGAE PPLREKFLRN MSQRAADILR DDLANRGPVR LSQVENEQKA ILLIVRRLAE TGE MVIGSG EDTYV

UniProtKB: Flagellar motor switch protein FliG

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Macromolecule #5: Chemotaxis protein CheY

MacromoleculeName: Chemotaxis protein CheY / type: protein_or_peptide / ID: 5 / Number of copies: 3 / Enantiomer: LEVO
Source (natural)Organism: Salmonella enterica subsp. enterica serovar Typhimurium str. LT2 (bacteria)
Molecular weightTheoretical: 14.177512 KDa
Recombinant expressionOrganism: Escherichia coli BL21(DE3) (bacteria)
SequenceString:
MADKELKFLV VDKFSTMRRI VRNLLKELGF NNVEEAEDGV DALNKLQAGG FGFIISDWNM PNMDGLELLK TIRADSAMSA LPVLMVTAE AKKENIIAAA QAGASGWVVK PFTAATLEEK LNKIFEKLGM

UniProtKB: Chemotaxis protein CheY

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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
Component:
ConcentrationFormulaName
11.7 mMTris-HCltris(hydroxymethyl)aminomethane hydrochloride
4.17 mMEDTAethylenediaminetetraacetic acid
0.083 % v/vTX-100octylphenol ethoxylate
25.0 mMNaClsodium chloride
GridModel: Quantifoil R0.6/1 / Material: GOLD / Mesh: 200 / Pretreatment - Type: GLOW DISCHARGE / Pretreatment - Time: 180 sec. / Pretreatment - Atmosphere: AIR
VitrificationCryogen name: ETHANE / Chamber humidity: 100 % / Chamber temperature: 277.15 K / Instrument: FEI VITROBOT MARK IV
Details: Blot time: 4 Blot force: 10 Wait time: 30 Blot total: 1 Drain time: 2.
DetailsThis sample was prepared by incubating the C ring-containing flagellar motor-hook complex with the constitutively active mutant of CheY (CheY**)

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Electron microscopy

MicroscopeFEI TITAN KRIOS
Specialist opticsEnergy filter - Name: TFS Selectris / Energy filter - Slit width: 10 eV
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 / Cs: 2.7 mm / 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: 46058 / Details: Particles were manually picked using cryoSPARC
Startup modelType of model: OTHER
Final reconstructionApplied symmetry - Point group: C1 (asymmetric) / Resolution.type: BY AUTHOR / Resolution: 4.4 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: cryoSPARC (ver. 4.1.1) / Details: C34 symmetry-expanded particles / Number images used: 956046
Initial angle assignmentType: MAXIMUM LIKELIHOOD / Software - Name: cryoSPARC (ver. 4.1.1)
Final angle assignmentType: MAXIMUM LIKELIHOOD / Software - Name: cryoSPARC (ver. 4.1.1)
FSC plot (resolution estimation)

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Atomic model buiding 1

Initial model
ChainPDB ID
source_name: AlphaFold, initial_model_type: in silico model
source_name: PDB, initial_model_type: experimental model

8xp0

source_name: PDB, initial_model_type: experimental model

2flw

RefinementSpace: REAL / Protocol: OTHER
Output model

PDB-8xp1:
Cryo-EM structure of the protomers of the C ring in the CW state

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