3GA0

CtBP1/BARS Gly172->Glu mutant structure: impairing NAD(H) binding and dimerization


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 3.40 Å
  • R-Value Free: 0.334 
  • R-Value Work: 0.262 
  • R-Value Observed: 0.270 

wwPDB Validation   3D Report Full Report


This is version 1.3 of the entry. See complete history


Literature

CtBP1/BARS Gly172-->Glu mutant structure: impairing NAD(H)-binding and dimerization

Nardini, M.Valente, C.Ricagno, S.Luini, A.Corda, D.Bolognesi, M.

(2009) Biochem Biophys Res Commun 381: 70-74

  • DOI: https://doi.org/10.1016/j.bbrc.2009.02.010
  • Primary Citation of Related Structures:  
    3GA0

  • PubMed Abstract: 

    C-terminal binding proteins (CtBPs) are multi-functional proteins involved in nuclear transcriptional co-repression, Golgi membrane fission, and synaptic ribbon formation. Binding of NAD(H) to CtBPs promotes dimerization. CtBP dimers act as a scaffold for multimeric protein complex formation, thus bridging transcriptional repressors and their targets in the nucleus. Based on size-exclusion chromatography experiments and on the crystal structure of the NAD(H)-free G172E CtBP mutant, we show here that absence of NAD(H) induces flexibility/backbone conformational changes at the dimerization interface and at the CtBP interdomain region. The results presented shed first light on the correlation between NAD(H)-binding and functional CtBP dimerization.


  • Organizational Affiliation

    Department of Biomolecular Sciences and Biotechnology, CNR-INFM and CIMAINA, University of Milano, Via Celoria 26, I-20133 Milano, Italy.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
C-terminal-binding protein 1358Rattus norvegicusMutation(s): 1 
Gene Names: Ctbp1BarsCtbp3
EC: 1.1.1
UniProt
Find proteins for Q9Z2F5 (Rattus norvegicus)
Explore Q9Z2F5 
Go to UniProtKB:  Q9Z2F5
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ9Z2F5
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 3.40 Å
  • R-Value Free: 0.334 
  • R-Value Work: 0.262 
  • R-Value Observed: 0.270 
  • Space Group: P 64 2 2
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 89.197α = 90
b = 89.197β = 90
c = 160.259γ = 120
Software Package:
Software NamePurpose
MOLREPphasing
REFMACrefinement
DENZOdata reduction
SCALEPACKdata scaling

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2009-04-21
    Type: Initial release
  • Version 1.1: 2011-07-13
    Changes: Version format compliance
  • Version 1.2: 2021-11-10
    Changes: Database references, Derived calculations
  • Version 1.3: 2023-11-01
    Changes: Data collection, Refinement description