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- PDB-8ucs: Cryo-EM structure of the flagellar MotAB stator bound to FliG -

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Basic information

Entry
Database: PDB / ID: 8ucs
TitleCryo-EM structure of the flagellar MotAB stator bound to FliG
Components
  • Flagellar motor switch protein FliG
  • Motility protein A
  • OmpA family protein
KeywordsMEMBRANE PROTEIN / flagella chemotaxis motility type III secretion system
Function / homology
Function and homology information


bacterial-type flagellum basal body / bacterial-type flagellum-dependent swarming motility / cytoskeletal motor activity / bacterial-type flagellum-dependent cell motility / proton transmembrane transport / chemotaxis / plasma membrane
Similarity search - Function
Motility protein A, N-terminal / Motility protein A N-terminal / Flagellar motor protein MotA, conserved site / Flagellar motor protein motA family signature. / : / 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 ...Motility protein A, N-terminal / Motility protein A N-terminal / Flagellar motor protein MotA, conserved site / Flagellar motor protein motA family signature. / : / 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 / Motility protein B-like, N-terminal domain / Membrane MotB of proton-channel complex MotA/MotB / MotA/TolQ/ExbB proton channel / MotA/TolQ/ExbB proton channel family / OmpA-like domain profile. / OmpA-like domain superfamily / OmpA family / OmpA-like domain
Similarity search - Domain/homology
Flagellar motor switch protein FliG / Motility protein A / OmpA family protein
Similarity search - Component
Biological speciesClostridium sporogenes (bacteria)
MethodELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 2.4 Å
AuthorsDeme, J.C. / Johnson, S. / Lea, S.M.
Funding support United States, 1items
OrganizationGrant numberCountry
National Institutes of Health/National Cancer Institute (NIH/NCI)CCR Core Funding for Lea Group United States
CitationJournal: Nat Microbiol / Year: 2024
Title: Structural basis of directional switching by the bacterial flagellum.
Authors: Steven Johnson / Justin C Deme / Emily J Furlong / Joseph J E Caesar / Fabienne F V Chevance / Kelly T Hughes / Susan M Lea /
Abstract: The bacterial flagellum is a macromolecular protein complex that harvests energy from uni-directional ion flow across the inner membrane to power bacterial swimming via rotation of the flagellar ...The bacterial flagellum is a macromolecular protein complex that harvests energy from uni-directional ion flow across the inner membrane to power bacterial swimming via rotation of the flagellar filament. Rotation is bi-directional, with binding of a cytoplasmic chemotactic response regulator controlling reversal, though the structural and mechanistic bases for rotational switching are not well understood. Here we present cryoelectron microscopy structures of intact Salmonella flagellar basal bodies (3.2-5.5 Å), including the cytoplasmic C-ring complexes required for power transmission, in both counter-clockwise and clockwise rotational conformations. These reveal 180° movements of both the N- and C-terminal domains of the FliG protein, which, when combined with a high-resolution cryoelectron microscopy structure of the MotAB stator, show that the stator shifts from the outside to the inside of the C-ring. This enables rotational switching and reveals how uni-directional ion flow across the inner membrane is used to accomplish bi-directional rotation of the flagellum.
History
DepositionSep 27, 2023Deposition site: RCSB / Processing site: RCSB
Revision 1.0Jan 24, 2024Provider: repository / Type: Initial release
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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: OmpA family protein
B: OmpA family protein
C: Motility protein A
D: Motility protein A
E: Motility protein A
F: Motility protein A
G: Motility protein A
H: Flagellar motor switch protein FliG
I: Flagellar motor switch protein FliG
J: Flagellar motor switch protein FliG


Theoretical massNumber of molelcules
Total (without water)242,73710
Polymers242,73710
Non-polymers00
Water362
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 OmpA family protein


Mass: 32078.861 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Clostridium sporogenes (bacteria) / Gene: CLOSPO_02354 / Production host: Escherichia coli (E. coli) / References: UniProt: J7SFK3
#2: Protein
Motility protein A


Mass: 28928.850 Da / Num. of mol.: 5
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Clostridium sporogenes (bacteria) / Gene: motA / Production host: Escherichia coli (E. coli) / References: UniProt: A0A7U4JQH9
#3: Protein Flagellar motor switch protein FliG


Mass: 11311.659 Da / Num. of mol.: 3
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Clostridium sporogenes (bacteria) / Gene: VT92_0222320 / Production host: Escherichia coli (E. coli) / References: UniProt: A0A1V9IMV5
#4: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Formula: H2O
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: MotAB stator complexed with FliG / Type: COMPLEX / Entity ID: #1-#3 / Source: RECOMBINANT
Source (natural)Organism: Clostridium sporogenes (bacteria)
Source (recombinant)Organism: Escherichia coli (E. coli)
Buffer solutionpH: 8
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: 2500 nm / Nominal defocus min: 1000 nm
Image recordingElectron dose: 56.5 e/Å2 / Film or detector model: FEI FALCON IV (4k x 4k)

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Processing

EM softwareName: PHENIX / Category: model refinement
CTF correctionType: PHASE FLIPPING AND AMPLITUDE CORRECTION
3D reconstructionResolution: 2.4 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 719539 / Symmetry type: POINT
Refine LS restraints
Refine-IDTypeDev idealNumber
ELECTRON MICROSCOPYf_bond_d0.00212783
ELECTRON MICROSCOPYf_angle_d0.47417225
ELECTRON MICROSCOPYf_dihedral_angle_d3.9421735
ELECTRON MICROSCOPYf_chiral_restr0.0352012
ELECTRON MICROSCOPYf_plane_restr0.0042184

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