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- PDB-9n4z: CCW Flagellar Switch Complex - FliF, FliG, FliM, and FliN forming... -

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Basic information

Entry
Database: PDB / ID: 9n4z
TitleCCW Flagellar Switch Complex - FliF, FliG, FliM, and FliN forming 34-mer C-ring from Salmonella
Components
  • Flagellar M-ring protein
  • Flagellar motor switch protein FliG
  • Flagellar motor switch protein FliM
  • Flagellar motor switch protein FliN
KeywordsMOTOR PROTEIN / C-ring / Bacterial / Chemotaxis / C ring / Flagellar Motor complex / switch complex / FliG / FliM / FliN / FliF
Function / homology
Function and homology information


bacterial-type flagellum basal body, MS ring / bacterial-type flagellum basal body / bacterial-type flagellum-dependent swarming motility / positive chemotaxis / cytoskeletal motor activity / bacterial-type flagellum-dependent cell motility / chemotaxis / plasma membrane
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
Similarity search - Domain/homology
Flagellar motor switch protein FliG / Flagellar M-ring protein / Flagellar motor switch protein FliM / Flagellar motor switch protein FliN
Similarity search - Component
Biological speciesSalmonella enterica subsp. enterica serovar Typhimurium (bacteria)
MethodELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3 Å
AuthorsSingh, P.K. / Iverson, T.M.
Funding support United States, 1items
OrganizationGrant numberCountry
National Institutes of Health/John E. Fogarty International Center (NIH/FIC)GM61606 United States
Citation
Journal: J Struct Biol / Year: 2025
Title: Improving CryoEM maps of symmetry-mismatched macromolecular assemblies: A case study on the flagellar motor.
Authors: Prashant K Singh / T M Iverson /
Abstract: Advances in cryo-electron microscopy instrumentation and sample preparation have significantly improved the ability to collect quality data for biomolecular structures. However, achieving resolutions ...Advances in cryo-electron microscopy instrumentation and sample preparation have significantly improved the ability to collect quality data for biomolecular structures. However, achieving resolutions consistent with data quality remains challenging in structures with symmetry mismatches. As a case study, the bacterial flagellar motor is a large complex essential for bacterial chemotaxis and virulence. This motor contains a smaller membrane-supramembrane ring (MS-ring) and a larger cytoplasmic ring (C-ring). These two features have a 33:34 symmetry mismatch when expressed in E. coli. Because close symmetry mismatches are the most difficult to deconvolute, this makes the flagellar motor an excellent model system to evaluate refinement strategies for symmetry mismatch. We compared the performance of masked refinement, local refinement, and particle subtracted refinement on the same data. We found that particle subtraction prior to refinement was critical for approaching the smaller MS-ring. Additional processing resulted in final resolutions of 3.1 Å for the MS-ring and 3.0 Å for the C-ring, which improves the resolution of the MS-ring by 0.3 Å and the resolution of the C-ring by 1.0 Å as compared to past work. Although particle subtraction is fairly well-established, it is rarely applied to problems of symmetry mismatch, making this case study a valuable demonstration of its utility in this context.
#1: Journal: Nat Microbiol / Year: 2024
Title: CryoEM structures reveal how the bacterial flagellum rotates and switches direction.
Authors: Prashant K Singh / Pankaj Sharma / Oshri Afanzar / Margo H Goldfarb / Elena Maklashina / Michael Eisenbach / Gary Cecchini / T M Iverson /
Abstract: Bacterial chemotaxis requires bidirectional flagellar rotation at different rates. Rotation is driven by a flagellar motor, which is a supercomplex containing multiple rings. Architectural ...Bacterial chemotaxis requires bidirectional flagellar rotation at different rates. Rotation is driven by a flagellar motor, which is a supercomplex containing multiple rings. Architectural uncertainty regarding the cytoplasmic C-ring, or 'switch', limits our understanding of how the motor transmits torque and direction to the flagellar rod. Here we report cryogenic electron microscopy structures for Salmonella enterica serovar typhimurium inner membrane MS-ring and C-ring in a counterclockwise pose (4.0 Å) and isolated C-ring in a clockwise pose alone (4.6 Å) and bound to a regulator (5.9 Å). Conformational differences between rotational poses include a 180° shift in FliF/FliG domains that rotates the outward-facing MotA/B binding site to inward facing. The regulator has specificity for the clockwise pose by bridging elements unique to this conformation. We used these structures to propose how the switch reverses rotation and transmits torque to the flagellum, which advances the understanding of bacterial chemotaxis and bidirectional motor rotation.
History
DepositionFeb 3, 2025Deposition site: RCSB / Processing site: RCSB
Revision 1.0Mar 19, 2025Provider: repository / Type: Initial release
Revision 1.0Mar 19, 2025Data content type: EM metadata / Data content type: EM metadata / Provider: repository / Type: Initial release
Revision 1.0Mar 19, 2025Data content type: Image / Data content type: Image / Provider: repository / Type: Initial release
Revision 1.0Mar 19, 2025Data content type: Primary map / Data content type: Primary map / Provider: repository / Type: Initial release
Revision 1.0Mar 19, 2025Data content type: Image / Data content type: Image / Provider: repository / Type: Initial release
Revision 1.0Mar 19, 2025Data content type: Primary map / Data content type: Primary map / Provider: repository / Type: Initial release
Revision 1.1Mar 26, 2025Group: Data collection / Database references / Category: citation / em_admin / Item: _citation.journal_volume / _em_admin.last_update
SupersessionApr 2, 2025ID: 8T8O
Revision 1.2Apr 2, 2025Group: Advisory / Data collection
Category: em_admin / em_obsolete / pdbx_database_PDB_obs_spr
Item: _em_admin.last_update
Revision 1.1Apr 2, 2025Data content type: EM metadata / Data content type: EM metadata / EM metadata / Group: Advisory / Experimental summary / Data content type: EM metadata / EM metadata / EM metadata
Category: em_admin / em_obsolete / pdbx_database_PDB_obs_spr
Data content type: EM metadata / Item: _em_admin.last_update

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
F: Flagellar M-ring protein
G: Flagellar motor switch protein FliG
M: Flagellar motor switch protein FliM
N: Flagellar motor switch protein FliN
P: Flagellar motor switch protein FliN
Q: Flagellar motor switch protein FliN
A: Flagellar M-ring protein
B: Flagellar motor switch protein FliG
C: Flagellar motor switch protein FliM
D: Flagellar motor switch protein FliN
E: Flagellar motor switch protein FliN
H: Flagellar motor switch protein FliN
I: Flagellar M-ring protein
J: Flagellar motor switch protein FliG
K: Flagellar motor switch protein FliM
L: Flagellar motor switch protein FliN
O: Flagellar motor switch protein FliN
R: Flagellar motor switch protein FliN
S: Flagellar M-ring protein
T: Flagellar motor switch protein FliG
V: Flagellar motor switch protein FliM
W: Flagellar motor switch protein FliN
X: Flagellar motor switch protein FliN
Y: Flagellar motor switch protein FliN
Z: Flagellar M-ring protein
AA: Flagellar motor switch protein FliG
BA: Flagellar motor switch protein FliM
CA: Flagellar motor switch protein FliN
DA: Flagellar motor switch protein FliN
EA: Flagellar motor switch protein FliN
FA: Flagellar M-ring protein
GA: Flagellar motor switch protein FliG
HA: Flagellar motor switch protein FliM
IA: Flagellar motor switch protein FliN
JA: Flagellar motor switch protein FliN
KA: Flagellar motor switch protein FliN
LA: Flagellar M-ring protein
MA: Flagellar motor switch protein FliG
NA: Flagellar motor switch protein FliM
OA: Flagellar motor switch protein FliN
PA: Flagellar motor switch protein FliN
QA: Flagellar motor switch protein FliN
RA: Flagellar M-ring protein
SA: Flagellar motor switch protein FliG
TA: Flagellar motor switch protein FliM
UA: Flagellar motor switch protein FliN
VA: Flagellar motor switch protein FliN
WA: Flagellar motor switch protein FliN
XA: Flagellar M-ring protein
YA: Flagellar motor switch protein FliG
ZA: Flagellar motor switch protein FliM
AB: Flagellar motor switch protein FliN
BB: Flagellar motor switch protein FliN
CB: Flagellar motor switch protein FliN
DB: Flagellar M-ring protein
EB: Flagellar motor switch protein FliG
FB: Flagellar motor switch protein FliM
GB: Flagellar motor switch protein FliN
HB: Flagellar motor switch protein FliN
IB: Flagellar motor switch protein FliN
JB: Flagellar M-ring protein
KB: Flagellar motor switch protein FliG
LB: Flagellar motor switch protein FliM
MB: Flagellar motor switch protein FliN
NB: Flagellar motor switch protein FliN
OB: Flagellar motor switch protein FliN
PB: Flagellar M-ring protein
QB: Flagellar motor switch protein FliG
RB: Flagellar motor switch protein FliM
SB: Flagellar motor switch protein FliN
TB: Flagellar motor switch protein FliN
UB: Flagellar motor switch protein FliN
VB: Flagellar M-ring protein
WB: Flagellar motor switch protein FliG
XB: Flagellar motor switch protein FliM
YB: Flagellar motor switch protein FliN
ZB: Flagellar motor switch protein FliN
AC: Flagellar motor switch protein FliN
BC: Flagellar M-ring protein
CC: Flagellar motor switch protein FliG
DC: Flagellar motor switch protein FliM
EC: Flagellar motor switch protein FliN
FC: Flagellar motor switch protein FliN
GC: Flagellar motor switch protein FliN
HC: Flagellar M-ring protein
IC: Flagellar motor switch protein FliG
JC: Flagellar motor switch protein FliM
KC: Flagellar motor switch protein FliN
LC: Flagellar motor switch protein FliN
MC: Flagellar motor switch protein FliN
NC: Flagellar M-ring protein
OC: Flagellar motor switch protein FliG
PC: Flagellar motor switch protein FliM
QC: Flagellar motor switch protein FliN
RC: Flagellar motor switch protein FliN
SC: Flagellar motor switch protein FliN
TC: Flagellar M-ring protein
UC: Flagellar motor switch protein FliG
VC: Flagellar motor switch protein FliM
WC: Flagellar motor switch protein FliN
XC: Flagellar motor switch protein FliN
YC: Flagellar motor switch protein FliN
ZC: Flagellar M-ring protein
AD: Flagellar motor switch protein FliG
BD: Flagellar motor switch protein FliM
CD: Flagellar motor switch protein FliN
DD: Flagellar motor switch protein FliN
ED: Flagellar motor switch protein FliN
FD: Flagellar M-ring protein
GD: Flagellar motor switch protein FliG
HD: Flagellar motor switch protein FliM
ID: Flagellar motor switch protein FliN
JD: Flagellar motor switch protein FliN
KD: Flagellar motor switch protein FliN
LD: Flagellar M-ring protein
MD: Flagellar motor switch protein FliG
ND: Flagellar motor switch protein FliM
OD: Flagellar motor switch protein FliN
PD: Flagellar motor switch protein FliN
QD: Flagellar motor switch protein FliN
RD: Flagellar M-ring protein
SD: Flagellar motor switch protein FliG
TD: Flagellar motor switch protein FliM
UD: Flagellar motor switch protein FliN
VD: Flagellar motor switch protein FliN
WD: Flagellar motor switch protein FliN
XD: Flagellar M-ring protein
YD: Flagellar motor switch protein FliG
ZD: Flagellar motor switch protein FliM
AE: Flagellar motor switch protein FliN
BE: Flagellar motor switch protein FliN
CE: Flagellar motor switch protein FliN
DE: Flagellar M-ring protein
EE: Flagellar motor switch protein FliG
FE: Flagellar motor switch protein FliM
GE: Flagellar motor switch protein FliN
HE: Flagellar motor switch protein FliN
IE: Flagellar motor switch protein FliN
JE: Flagellar M-ring protein
KE: Flagellar motor switch protein FliG
LE: Flagellar motor switch protein FliM
ME: Flagellar motor switch protein FliN
NE: Flagellar motor switch protein FliN
OE: Flagellar motor switch protein FliN
PE: Flagellar M-ring protein
QE: Flagellar motor switch protein FliG
RE: Flagellar motor switch protein FliM
SE: Flagellar motor switch protein FliN
TE: Flagellar motor switch protein FliN
UE: Flagellar motor switch protein FliN
VE: Flagellar M-ring protein
WE: Flagellar motor switch protein FliG
XE: Flagellar motor switch protein FliM
YE: Flagellar motor switch protein FliN
ZE: Flagellar motor switch protein FliN
AF: Flagellar motor switch protein FliN
BF: Flagellar M-ring protein
CF: Flagellar motor switch protein FliG
DF: Flagellar motor switch protein FliM
EF: Flagellar motor switch protein FliN
FF: Flagellar motor switch protein FliN
GF: Flagellar motor switch protein FliN
HF: Flagellar M-ring protein
IF: Flagellar motor switch protein FliG
JF: Flagellar motor switch protein FliM
KF: Flagellar motor switch protein FliN
LF: Flagellar motor switch protein FliN
MF: Flagellar motor switch protein FliN
NF: Flagellar M-ring protein
OF: Flagellar motor switch protein FliG
PF: Flagellar motor switch protein FliM
QF: Flagellar motor switch protein FliN
RF: Flagellar motor switch protein FliN
SF: Flagellar motor switch protein FliN
TF: Flagellar M-ring protein
UF: Flagellar motor switch protein FliG
VF: Flagellar motor switch protein FliM
WF: Flagellar motor switch protein FliN
XF: Flagellar motor switch protein FliN
YF: Flagellar motor switch protein FliN
ZF: Flagellar M-ring protein
AG: Flagellar motor switch protein FliG
BG: Flagellar motor switch protein FliM
CG: Flagellar motor switch protein FliN
DG: Flagellar motor switch protein FliN
EG: Flagellar motor switch protein FliN
FG: Flagellar M-ring protein
GG: Flagellar motor switch protein FliG
HG: Flagellar motor switch protein FliM
IG: Flagellar motor switch protein FliN
JG: Flagellar motor switch protein FliN
KG: Flagellar motor switch protein FliN
LG: Flagellar M-ring protein
MG: Flagellar motor switch protein FliG
NG: Flagellar motor switch protein FliM
OG: Flagellar motor switch protein FliN
PG: Flagellar motor switch protein FliN
QG: Flagellar motor switch protein FliN
RG: Flagellar M-ring protein
SG: Flagellar motor switch protein FliG
TG: Flagellar motor switch protein FliM
UG: Flagellar motor switch protein FliN
VG: Flagellar motor switch protein FliN
WG: Flagellar motor switch protein FliN


Theoretical massNumber of molelcules
Total (without water)6,136,767204
Polymers6,136,767204
Non-polymers00
Water00
1


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

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Components

#1: Protein ...
Flagellar M-ring protein / FliF


Mass: 61295.645 Da / Num. of mol.: 34
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Salmonella enterica subsp. enterica serovar Typhimurium (bacteria)
Gene: fliF, fla AII.1, fla BI, STM1969 / Production host: Escherichia coli BL21(DE3) (bacteria) / References: UniProt: P15928
#2: Protein ...
Flagellar motor switch protein FliG


Mass: 36890.957 Da / Num. of mol.: 34
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Salmonella enterica subsp. enterica serovar Typhimurium (bacteria)
Gene: fliG, fla AII.2, fla BII, STM1970 / Production host: Escherichia coli BL21(DE3) (bacteria) / References: UniProt: P0A1J9
#3: Protein ...
Flagellar motor switch protein FliM


Mass: 37901.066 Da / Num. of mol.: 34
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Salmonella enterica subsp. enterica serovar Typhimurium (bacteria)
Gene: fliM, cheC2, fla AII, fla QII, STM1976 / Production host: Escherichia coli BL21(DE3) (bacteria) / References: UniProt: P26418
#4: Protein ...
Flagellar motor switch protein FliN


Mass: 14801.823 Da / Num. of mol.: 102
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Salmonella enterica subsp. enterica serovar Typhimurium (bacteria)
Gene: fliN, flaN, motD, STM1977 / Production host: Escherichia coli BL21(DE3) (bacteria) / References: UniProt: P26419
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: Bacterial flagellar motor switch complex / Type: COMPLEX / Entity ID: all / Source: RECOMBINANT
Molecular weightValue: 4.103 MDa / Experimental value: NO
Source (natural)Organism: Salmonella enterica subsp. enterica serovar Typhimurium (bacteria)
Source (recombinant)Organism: Escherichia coli BL21(DE3) (bacteria)
Buffer solutionpH: 7.4
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: OTHER
Electron lensMode: BRIGHT FIELD / Nominal defocus max: 2000 nm / Nominal defocus min: 1000 nm
Image recordingElectron dose: 51.557 e/Å2 / Film or detector model: GATAN K3 (6k x 4k)

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Processing

EM software
IDNameVersionCategory
7Coot0.9model fitting
9PHENIX1.20.1-4487-000model refinement
13cryoSPARC4.5.33D reconstruction
CTF correctionType: PHASE FLIPPING AND AMPLITUDE CORRECTION
3D reconstructionResolution: 3 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 20863 / Symmetry type: POINT

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