6EKH

Crystal structure of activated CheY from Methanoccocus maripaludis


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.65 Å
  • R-Value Free: 0.315 
  • R-Value Work: 0.284 
  • R-Value Observed: 0.286 

wwPDB Validation   3D Report Full Report


This is version 1.4 of the entry. See complete history


Literature

Structure and function of the archaeal response regulator CheY.

Quax, T.E.F.Altegoer, F.Rossi, F.Li, Z.Rodriguez-Franco, M.Kraus, F.Bange, G.Albers, S.V.

(2018) Proc Natl Acad Sci U S A 115: E1259-E1268

  • DOI: https://doi.org/10.1073/pnas.1716661115
  • Primary Citation of Related Structures:  
    6EKG, 6EKH

  • PubMed Abstract: 

    Motility is a central feature of many microorganisms and provides an efficient strategy to respond to environmental changes. Bacteria and archaea have developed fundamentally different rotary motors enabling their motility, termed flagellum and archaellum, respectively. Bacterial motility along chemical gradients, called chemotaxis, critically relies on the response regulator CheY, which, when phosphorylated, inverses the rotational direction of the flagellum via a switch complex at the base of the motor. The structural difference between archaellum and flagellum and the presence of functional CheY in archaea raises the question of how the CheY protein changed to allow communication with the archaeal motility machinery. Here we show that archaeal CheY shares the overall structure and mechanism of magnesium-dependent phosphorylation with its bacterial counterpart. However, bacterial and archaeal CheY differ in the electrostatic potential of the helix α4. The helix α4 is important in bacteria for interaction with the flagellar switch complex, a structure that is absent in archaea. We demonstrated that phosphorylation-dependent activation, and conserved residues in the archaeal CheY helix α4, are important for interaction with the archaeal-specific adaptor protein CheF. This forms a bridge between the chemotaxis system and the archaeal motility machinery. Conclusively, archaeal CheY proteins conserved the central mechanistic features between bacteria and archaea, but differ in the helix α4 to allow binding to an archaellum-specific interaction partner.


  • Organizational Affiliation

    Molecular Biology of Archaea, Faculty of Biology, University of Freiburg, 79104 Freiburg, Germany.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Chemotaxis protein CheYA [auth Y]123Methanococcus maripaludisMutation(s): 0 
Gene Names: cheYMMP0933
UniProt
Find proteins for Q6LYQ5 (Methanococcus maripaludis (strain S2 / LL))
Explore Q6LYQ5 
Go to UniProtKB:  Q6LYQ5
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ6LYQ5
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.65 Å
  • R-Value Free: 0.315 
  • R-Value Work: 0.284 
  • R-Value Observed: 0.286 
  • Space Group: P 31 2 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 71.332α = 90
b = 71.332β = 90
c = 77.115γ = 120
Software Package:
Software NamePurpose
PHENIXrefinement
XDSdata reduction
Aimlessdata scaling
PHASERphasing

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2018-01-31
    Type: Initial release
  • Version 1.1: 2018-02-14
    Changes: Data collection
  • Version 1.2: 2018-02-21
    Changes: Database references
  • Version 1.3: 2019-02-20
    Changes: Advisory, Data collection, Derived calculations
  • Version 1.4: 2024-01-17
    Changes: Data collection, Database references, Derived calculations, Refinement description