6YKM

Structure of C. jejuni MotAB


Experimental Data Snapshot

  • Method: ELECTRON MICROSCOPY
  • Resolution: 3.10 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

Structure and Function of Stator Units of the Bacterial Flagellar Motor.

Santiveri, M.Roa-Eguiara, A.Kuhne, C.Wadhwa, N.Hu, H.Berg, H.C.Erhardt, M.Taylor, N.M.I.

(2020) Cell 183: 244-257.e16

  • DOI: https://doi.org/10.1016/j.cell.2020.08.016
  • Primary Citation of Related Structures:  
    6YKM, 6YKP, 6YKR

  • PubMed Abstract: 

    Many bacteria use the flagellum for locomotion and chemotaxis. Its bidirectional rotation is driven by a membrane-embedded motor, which uses energy from the transmembrane ion gradient to generate torque at the interface between stator units and rotor. The structural organization of the stator unit (MotAB), its conformational changes upon ion transport, and how these changes power rotation of the flagellum remain unknown. Here, we present ~3 Å-resolution cryoelectron microscopy reconstructions of the stator unit in different functional states. We show that the stator unit consists of a dimer of MotB surrounded by a pentamer of MotA. Combining structural data with mutagenesis and functional studies, we identify key residues involved in torque generation and present a detailed mechanistic model for motor function and switching of rotational direction.


  • Organizational Affiliation

    Structural Biology of Molecular Machines Group, Protein Structure & Function Program, Novo Nordisk Foundation Center for Protein Research, Faculty of Health and Medical Sciences, University of Copenhagen, Blegdamsvej 3B, 2200 Copenhagen, Denmark.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Chemotaxis protein MotA, putative
A, B, C, D, E
258Campylobacter jejuni subsp. jejuni 81-176Mutation(s): 0 
Gene Names: CJJ81176_0359
Membrane Entity: Yes 
UniProt
Find proteins for A0A0H3PAV1 (Campylobacter jejuni subsp. jejuni serotype O:23/36 (strain 81-176))
Explore A0A0H3PAV1 
Go to UniProtKB:  A0A0H3PAV1
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupA0A0H3PAV1
Sequence Annotations
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  • Reference Sequence
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 2
MoleculeChains Sequence LengthOrganismDetailsImage
Chemotaxis protein MotB, putative
F, G
291Campylobacter jejuni subsp. jejuni 81-176Mutation(s): 0 
Gene Names: CJJ81176_0358
Membrane Entity: Yes 
UniProt
Find proteins for A0A0H3PBX6 (Campylobacter jejuni subsp. jejuni serotype O:23/36 (strain 81-176))
Explore A0A0H3PBX6 
Go to UniProtKB:  A0A0H3PBX6
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupA0A0H3PBX6
Sequence Annotations
Expand
  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: ELECTRON MICROSCOPY
  • Resolution: 3.10 Å
  • Aggregation State: PARTICLE 
  • Reconstruction Method: SINGLE PARTICLE 
EM Software:
TaskSoftware PackageVersion
RECONSTRUCTIONRELION3.0

Structure Validation

View Full Validation Report



Entry History & Funding Information

Deposition Data


Funding OrganizationLocationGrant Number
Novo Nordisk FoundationDenmarkNNF14CC0001
Danish Council for Independent ResearchDenmark8123-00002B

Revision History  (Full details and data files)

  • Version 1.0: 2020-09-30
    Type: Initial release
  • Version 1.1: 2020-10-14
    Changes: Database references
  • Version 1.2: 2024-05-22
    Changes: Data collection, Database references