5IDJ

Bifunctional histidine kinase CckA (domains DHp-CA) in complex with ADP/Mg2+


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 3.02 Å
  • R-Value Free: 0.289 
  • R-Value Work: 0.239 
  • R-Value Observed: 0.242 

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Ligand Structure Quality Assessment 


This is version 2.2 of the entry. See complete history


Literature

Cyclic di-GMP mediates a histidine kinase/phosphatase switch by noncovalent domain cross-linking.

Dubey, B.N.Lori, C.Ozaki, S.Fucile, G.Plaza-Menacho, I.Jenal, U.Schirmer, T.

(2016) Sci Adv 2: e1600823-e1600823

  • DOI: https://doi.org/10.1126/sciadv.1600823
  • Primary Citation of Related Structures:  
    5IDJ, 5IDM

  • PubMed Abstract: 

    Histidine kinases are key components of regulatory networks in bacteria. Although many of these enzymes are bifunctional, mediating both phosphorylation and dephosphorylation of downstream targets, the molecular details of this central regulatory switch are unclear. We showed recently that the universal second messenger cyclic di-guanosine monophosphate (c-di-GMP) drives Caulobacter crescentus cell cycle progression by forcing the cell cycle kinase CckA from its default kinase into phosphatase mode. We use a combination of structure determination, modeling, and functional analysis to demonstrate that c-di-GMP reciprocally regulates the two antagonistic CckA activities through noncovalent cross-linking of the catalytic domain with the dimerization histidine phosphotransfer (DHp) domain. We demonstrate that both c-di-GMP and ADP (adenosine diphosphate) promote phosphatase activity and propose that c-di-GMP stabilizes the ADP-bound quaternary structure, which allows the receiver domain to access the dimeric DHp stem for dephosphorylation. In silico analyses predict that c-di-GMP control is widespread among bacterial histidine kinases, arguing that it can replace or modulate canonical transmembrane signaling.


  • Organizational Affiliation

    Focal Area of Structural Biology and Biophysics, University of Basel, CH-4056 Basel, Switzerland.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Histidine kinase242Caulobacter vibrioidesMutation(s): 0 
Gene Names: cckA
EC: 2.7.13.3
UniProt
Find proteins for Q9X688 (Caulobacter vibrioides)
Explore Q9X688 
Go to UniProtKB:  Q9X688
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ9X688
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 3.02 Å
  • R-Value Free: 0.289 
  • R-Value Work: 0.239 
  • R-Value Observed: 0.242 
  • Space Group: P 63 2 2
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 164.856α = 90
b = 164.856β = 90
c = 48.001γ = 120
Software Package:
Software NamePurpose
PHENIXrefinement
iMOSFLMdata reduction
SCALAdata scaling
PHASERphasing
PDB_EXTRACTdata extraction

Structure Validation

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Ligand Structure Quality Assessment 


Entry History & Funding Information

Deposition Data


Funding OrganizationLocationGrant Number
Swiss National Science FoundationSwitzerland31003A-138414

Revision History  (Full details and data files)

  • Version 1.0: 2016-10-05
    Type: Initial release
  • Version 1.1: 2017-09-13
    Changes: Advisory, Author supporting evidence
  • Version 1.2: 2018-10-24
    Changes: Advisory, Data collection, Derived calculations
  • Version 2.0: 2022-09-07
    Changes: Advisory, Atomic model, Author supporting evidence, Data collection, Database references, Other, Polymer sequence, Refinement description, Structure summary
  • Version 2.1: 2022-09-21
    Changes: Database references, Refinement description
  • Version 2.2: 2024-02-07
    Changes: Data collection, Refinement description