4KP4

Deciphering cis-trans directionality and visualizing autophosphorylation in histidine kinases.


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 3.00 Å
  • R-Value Free: 0.234 
  • R-Value Work: 0.194 
  • R-Value Observed: 0.196 

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Ligand Structure Quality Assessment 


This is version 1.4 of the entry. See complete history


Literature

Visualizing autophosphorylation in histidine kinases.

Casino, P.Miguel-Romero, L.Marina, A.

(2014) Nat Commun 5: 3258-3258

  • DOI: https://doi.org/10.1038/ncomms4258
  • Primary Citation of Related Structures:  
    4KP4

  • PubMed Abstract: 

    Reversible protein phosphorylation is the most widespread regulatory mechanism in signal transduction. Autophosphorylation in a dimeric sensor histidine kinase is the first step in two-component signalling, the predominant signal-transduction device in bacteria. Despite being the most abundant sensor kinases in nature, the molecular bases of the histidine kinase autophosphorylation mechanism are still unknown. Furthermore, it has been demonstrated that autophosphorylation can occur in two directions, cis (intrasubunit) or trans (intersubunit) within the dimeric histidine kinase. Here, we present the crystal structure of the complete catalytic machinery of a chimeric histidine kinase. The structure shows an asymmetric histidine kinase dimer where one subunit is caught performing the autophosphorylation reaction. A structure-guided functional analysis on HK853 and EnvZ, two prototypical cis- and trans-phosphorylating histidine kinases, has allowed us to decipher the catalytic mechanism of histidine kinase autophosphorylation, which seems to be common independently of the reaction directionality.


  • Organizational Affiliation

    1] Department of Genomic and Proteomic, Instituto de Biomedicina de Valencia (IBV-CSIC), Jaume Roig 11, 46010 Valencia, Spain [2] Department of Structural Biology, Institut de Biología Molecular de Barcelona (IBMB-CSIC), Baldiri Reixac, 4-8, Torre R, 3era Planta, 08028 Barcelona, Spain.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Osmolarity sensor protein EnvZ, Histidine kinase
A, B
236Escherichia coli K-12Thermotoga maritima MSB8Mutation(s): 0 
Gene Names: envZThemaDRAFT_0449TM_0853b3404JW3367ompBperAtpo
EC: 2.7.13.3
UniProt
Find proteins for P0AEJ4 (Escherichia coli (strain K12))
Explore P0AEJ4 
Go to UniProtKB:  P0AEJ4
Find proteins for Q9WZV7 (Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8))
Explore Q9WZV7 
Go to UniProtKB:  Q9WZV7
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupsQ9WZV7P0AEJ4
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 3.00 Å
  • R-Value Free: 0.234 
  • R-Value Work: 0.194 
  • R-Value Observed: 0.196 
  • Space Group: P 65 2 2
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 163.686α = 90
b = 163.686β = 90
c = 130.093γ = 120
Software Package:
Software NamePurpose
PHASERphasing
REFMACrefinement
XDSdata reduction
SCALAdata scaling

Structure Validation

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Ligand Structure Quality Assessment 


Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2014-02-12
    Type: Initial release
  • Version 1.1: 2014-02-19
    Changes: Database references
  • Version 1.2: 2017-08-16
    Changes: Refinement description, Source and taxonomy
  • Version 1.3: 2017-11-15
    Changes: Refinement description
  • Version 1.4: 2024-02-28
    Changes: Data collection, Database references, Derived calculations