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- PDB-8zds: Structure of the Salmonella flagellar MS-ring with C11 symmetry a... -

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Basic information

Entry
Database: PDB / ID: 8zds
TitleStructure of the Salmonella flagellar MS-ring with C11 symmetry applied
ComponentsFlagellar M-ring protein
KeywordsMOTOR PROTEIN / Bacterial flagellum / flagellar assembly / electron Cryomicroscopy / MS-ring / type III secretion system / Salmonella
Function / homology
Function and homology information


bacterial-type flagellum basal body, MS ring / cytoskeletal motor activity / bacterial-type flagellum-dependent cell motility / plasma membrane
Similarity search - Function
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 M-ring protein
Similarity search - Component
Biological speciesSalmonella enterica subsp. enterica serovar Typhimurium (bacteria)
MethodELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.1 Å
AuthorsKinoshita, M. / Makino, F. / Miyata, T. / Imada, K. / Minamino, T. / Namba, K.
Funding support Japan, 10items
OrganizationGrant numberCountry
Japan Society for the Promotion of Science (JSPS)JP20K15749 Japan
Japan Society for the Promotion of Science (JSPS)JP22K06162 Japan
Japan Society for the Promotion of Science (JSPS)JP19H03182 Japan
Japan Society for the Promotion of Science (JSPS)JP22H02573 Japan
Japan Society for the Promotion of Science (JSPS)JP22K19274 Japan
Japan Agency for Medical Research and Development (AMED)JP19am0101117 Japan
Japan Agency for Medical Research and Development (AMED)JP21am0101117 Japan
Japan Agency for Medical Research and Development (AMED)JP17pc0101020 Japan
Ministry of Education, Culture, Sports, Science and Technology (Japan)JP20H05532 Japan
Ministry of Education, Culture, Sports, Science and Technology (Japan)JP22H04844 Japan
CitationJournal: Commun Biol / Year: 2025
Title: Structural basis for assembly and function of the Salmonella flagellar MS-ring with three different symmetries.
Authors: Miki Kinoshita / Fumiaki Makino / Tomoko Miyata / Katsumi Imada / Keiichi Namba / Tohru Minamino /
Abstract: The flagellar MS-ring is the initial template for flagellar assembly and houses the flagellar protein export complex. The MS-ring has three parts of different symmetries within the ring structure by ...The flagellar MS-ring is the initial template for flagellar assembly and houses the flagellar protein export complex. The MS-ring has three parts of different symmetries within the ring structure by assembly of FliF subunits in two different conformations with distinct arrangements of three ring-building motifs, RBM1, RBM2, and RBM3. However, it remains unknown how these symmetries are generated. A combination of cryoEM structure and structure-based mutational analyses demonstrates that the well-conserved DQxGxxL motif in the RBM2-RBM3 hinge loop allows RBM2 to take two different orientations relative to RBM3. Of 34 FliF subunits of the MS-ring in the basal body, 23 RBM2 domains form an inner ring with a central pore that accommodates the flagellar protein export complex, and the remaining 11 RBM2 domains form 11 cog-like structures together with RBM1 domains just outside the inner RBM2-ring. We propose that a dimer of FliF with two different conformations initiates MS-ring assembly.
History
DepositionMay 3, 2024Deposition site: PDBJ / Processing site: PDBJ
Revision 1.0Jan 1, 2025Provider: repository / Type: Initial release
Revision 1.1Apr 23, 2025Group: Data collection / Database references / Category: citation / citation_author / em_admin
Item: _citation.journal_volume / _citation.page_first ..._citation.journal_volume / _citation.page_first / _citation.page_last / _citation.pdbx_database_id_DOI / _citation.pdbx_database_id_PubMed / _citation_author.identifier_ORCID / _citation_author.name / _em_admin.last_update

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Flagellar M-ring protein
B: Flagellar M-ring protein
C: Flagellar M-ring protein
D: Flagellar M-ring protein
E: Flagellar M-ring protein
F: Flagellar M-ring protein
G: Flagellar M-ring protein
H: Flagellar M-ring protein
I: Flagellar M-ring protein
J: Flagellar M-ring protein
K: Flagellar M-ring protein
L: Flagellar M-ring protein
M: Flagellar M-ring protein
N: Flagellar M-ring protein
O: Flagellar M-ring protein
P: Flagellar M-ring protein
Q: Flagellar M-ring protein
R: Flagellar M-ring protein
S: Flagellar M-ring protein
T: Flagellar M-ring protein
U: Flagellar M-ring protein
V: Flagellar M-ring protein
W: Flagellar M-ring protein
X: Flagellar M-ring protein
Y: Flagellar M-ring protein
Z: Flagellar M-ring protein
a: Flagellar M-ring protein
b: Flagellar M-ring protein
c: Flagellar M-ring protein
d: Flagellar M-ring protein
e: Flagellar M-ring protein
f: Flagellar M-ring protein
g: Flagellar M-ring protein


Theoretical massNumber of molelcules
Total (without water)2,022,75633
Polymers2,022,75633
Non-polymers00
Water00
1


  • Idetical with deposited unit
  • defined by author&software
  • Evidence: electron microscopy, not applicable
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1

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Components

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


Mass: 61295.645 Da / Num. of mol.: 33
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: Salmonella enterica subsp. enterica serovar Typhimurium (bacteria)
References: UniProt: P15928
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: Structure of the Salmonella flagellar MS-ring with C11 symmetry applied
Type: COMPLEX / Entity ID: all / Source: RECOMBINANT
Molecular weightExperimental value: NO
Source (natural)Organism: Salmonella enterica subsp. enterica serovar Typhimurium str. LT2 (bacteria)
Source (recombinant)Organism: Salmonella enterica subsp. enterica serovar Typhimurium str. LT2 (bacteria)
Buffer solutionpH: 8
Buffer component
IDConc.NameFormulaBuffer-ID
150 mMsodium chlorideNaCl1
225 mMImidazoleImidazole1
350 mMtris(hydroxymethyl)aminomethaneTris1
40.05 %Lauryl maltose neopentyl glycolLMNG1
50.05 %Triton X-100Triton1
SpecimenEmbedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES
Specimen supportGrid material: COPPER / Grid mesh size: 200 divisions/in. / Grid type: Quantifoil R0.6/1
VitrificationInstrument: FEI VITROBOT MARK III / Cryogen name: ETHANE / Humidity: 100 % / Chamber temperature: 277 K

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Electron microscopy imaging

MicroscopyModel: JEOL CRYO ARM 300
Electron gunElectron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM
Electron lensMode: BRIGHT FIELD / Nominal magnification: 50000 X / Nominal defocus max: 2500 nm / Nominal defocus min: 500 nm / Cs: 2.7 mm / Alignment procedure: COMA FREE
Specimen holderCryogen: NITROGEN / Specimen holder model: JEOL CRYOSPECPORTER
Image recordingElectron dose: 40 e/Å2 / Film or detector model: GATAN K3 (6k x 4k) / Num. of real images: 4885
EM imaging opticsEnergyfilter name: In-column Omega Filter / Energyfilter slit width: 20 eV
Image scansSampling size: 5 µm / Width: 5760 / Height: 4092

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Processing

EM software
IDNameVersionCategoryFitting-ID
7UCSF Chimera8.6.10model fitting1
13PHENIX1.20.1-4487model refinement1
14Coot0.9.8.7model refinement1
CTF correctionType: PHASE FLIPPING AND AMPLITUDE CORRECTION
Particle selectionNum. of particles selected: 1015741
SymmetryPoint symmetry: C11 (11 fold cyclic)
3D reconstructionResolution: 3.1 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 70250 / Algorithm: FOURIER SPACE / Symmetry type: POINT
Atomic model building
IDProtocolSpace
1FLEXIBLE FITREAL
2
Atomic model building
IDPDB-ID 3D fitting-IDAccession codeDetailsInitial refinement model-IDSource nameType
17D84

7d84

17D847D841PDBexperimental model
27CIK

7cik

17CIK7CIK2PDBexperimental model
32
42
Refine LS restraints
Refine-IDTypeDev idealNumber
ELECTRON MICROSCOPYf_bond_d0.00470422
ELECTRON MICROSCOPYf_angle_d0.64295337
ELECTRON MICROSCOPYf_dihedral_angle_d4.7079713
ELECTRON MICROSCOPYf_chiral_restr0.04111132
ELECTRON MICROSCOPYf_plane_restr0.00412716

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