1B9X

STRUCTURAL ANALYSIS OF PHOSDUCIN AND ITS PHOSPHORYLATION-REGULATED INTERACTION WITH TRANSDUCIN


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 3.00 Å
  • R-Value Free: 0.261 
  • R-Value Work: 0.217 

wwPDB Validation   3D Report Full Report


This is version 1.4 of the entry. See complete history


Literature

A molecular mechanism for the phosphorylation-dependent regulation of heterotrimeric G proteins by phosducin.

Gaudet, R.Savage, J.R.McLaughlin, J.N.Willardson, B.M.Sigler, P.B.

(1999) Mol Cell 3: 649-660

  • DOI: https://doi.org/10.1016/s1097-2765(00)80358-5
  • Primary Citation of Related Structures:  
    1B9X, 1B9Y

  • PubMed Abstract: 

    Visual signal transduction is a nearly noise-free process that is exquisitely well regulated over a wide dynamic range of light intensity. A key component in dark/light adaptation is phosducin, a phosphorylatable protein that modulates the amount of transducin heterotrimer (Gt alpha beta gamma) available through sequestration of the beta gamma subunits (Gt beta gamma). The structure of the phosphophosducin/Gt beta gamma complex combined with mutational and biophysical analysis provides a stereochemical mechanism for the regulation of the phosducin-Gt beta gamma interaction. Phosphorylation of serine 73 causes an order-to-disorder transition of a 20-residue stretch, including the phosphorylation site, by disrupting a helix-capping motif. This transition disrupts phosducin's interface with Gt beta gamma, leading to the release of unencumbered Gt beta gamma, which reassociates with the membrane and Gt alpha to form a signaling-competent Gt alpha beta gamma heterotrimer.


  • Organizational Affiliation

    Department of Molecular Biophysics, Howard Hughes Medical Institute, Yale University, New Haven, Connecticut 06511, USA.


Macromolecules
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Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
PROTEIN (TRANSDUCIN)340Bos taurusMutation(s): 0 
UniProt
Find proteins for P62871 (Bos taurus)
Explore P62871 
Go to UniProtKB:  P62871
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP62871
Sequence Annotations
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  • Reference Sequence
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Entity ID: 2
MoleculeChains Sequence LengthOrganismDetailsImage
PROTEIN (TRANSDUCIN)68Bos taurusMutation(s): 0 
Membrane Entity: Yes 
UniProt
Find proteins for P02698 (Bos taurus)
Explore P02698 
Go to UniProtKB:  P02698
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UniProt GroupP02698
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  • Reference Sequence
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Entity ID: 3
MoleculeChains Sequence LengthOrganismDetailsImage
PROTEIN (PHOSDUCIN)246Rattus norvegicusMutation(s): 0 
Gene Names: RAT PDC
UniProt
Find proteins for P20942 (Rattus norvegicus)
Explore P20942 
Go to UniProtKB:  P20942
Entity Groups  
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UniProt GroupP20942
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 3.00 Å
  • R-Value Free: 0.261 
  • R-Value Work: 0.217 
  • Space Group: P 21 21 21
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 76.04α = 90
b = 89.33β = 90
c = 100.15γ = 90
Software Package:
Software NamePurpose
CNSrefinement
DENZOdata reduction
SCALEPACKdata scaling
CNSphasing

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 1999-02-23
    Type: Initial release
  • Version 1.1: 2008-04-26
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance
  • Version 1.3: 2019-11-06
    Changes: Data collection, Database references
  • Version 1.4: 2023-08-09
    Changes: Data collection, Database references, Derived calculations, Refinement description