6YSF

Structure of the flagellar MotAB stator complex from Clostridium sporogenes


Experimental Data Snapshot

  • Method: ELECTRON MICROSCOPY
  • Resolution: 3.40 Å
  • Aggregation State: PARTICLE 
  • Reconstruction Method: SINGLE PARTICLE 

wwPDB Validation   3D Report Full Report


This is version 1.2 of the entry. See complete history


Literature

Structures of the stator complex that drives rotation of the bacterial flagellum.

Deme, J.C.Johnson, S.Vickery, O.Aron, A.Monkhouse, H.Griffiths, T.James, R.H.Berks, B.C.Coulton, J.W.Stansfeld, P.J.Lea, S.M.

(2020) Nat Microbiol 5: 1553-1564

  • DOI: https://doi.org/10.1038/s41564-020-0788-8
  • Primary Citation of Related Structures:  
    6YSF, 6YSL

  • PubMed Abstract: 

    The bacterial flagellum is the prototypical protein nanomachine and comprises a rotating helical propeller attached to a membrane-embedded motor complex. The motor consists of a central rotor surrounded by stator units that couple ion flow across the cytoplasmic membrane to generate torque. Here, we present the structures of the stator complexes from Clostridium sporogenes, Bacillus subtilis and Vibrio mimicus, allowing interpretation of the extensive body of data on stator mechanism. The structures reveal an unexpected asymmetric A 5 B 2 subunit assembly where the five A subunits enclose the two B subunits. Comparison to structures of other ion-driven motors indicates that this A 5 B 2 architecture is fundamental to bacterial systems that couple energy from ion flow to generate mechanical work at a distance and suggests that such events involve rotation in the motor structures.


  • Organizational Affiliation

    Sir William Dunn School of Pathology, University of Oxford, Oxford, UK.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Chemotaxis motB protein
A, B
251Clostridium sporogenesMutation(s): 0 
Gene Names: motBNCTC13020_02207NCTC534_01101VT92_0222420VT96_0225960
Membrane Entity: Yes 
UniProt
Find proteins for A0A1V9IL35 (Clostridium sporogenes)
Explore A0A1V9IL35 
Go to UniProtKB:  A0A1V9IL35
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupA0A1V9IL35
Sequence Annotations
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  • Reference Sequence
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 2
MoleculeChains Sequence LengthOrganismDetailsImage
Chemotaxis MotA proteinC [auth E],
D [auth C],
E [auth D],
F,
G
270Clostridium sporogenesMutation(s): 0 
Gene Names: motANCTC13020_02206
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
Sequence Annotations
Expand
  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: ELECTRON MICROSCOPY
  • Resolution: 3.40 Å
  • Aggregation State: PARTICLE 
  • Reconstruction Method: SINGLE PARTICLE 
EM Software:
TaskSoftware PackageVersion
RECONSTRUCTIONRELION3.1
MODEL REFINEMENTPHENIX

Structure Validation

View Full Validation Report



Entry History & Funding Information

Deposition Data


Funding OrganizationLocationGrant Number
Wellcome TrustUnited Kingdom107929/Z/15/Z
Wellcome TrustUnited Kingdom100298/Z/12/Z
Wellcome TrustUnited Kingdom201536/Z/16/Z
Medical Research Council (MRC, United Kingdom)United KingdomMR/M011984/1

Revision History  (Full details and data files)

  • Version 1.0: 2020-08-12
    Type: Initial release
  • Version 1.1: 2020-09-30
    Changes: Database references
  • Version 1.2: 2020-12-02
    Changes: Database references