1HBX

Ternary Complex of SAP-1 and SRF with specific SRE DNA


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 3.15 Å
  • R-Value Free: 0.285 
  • R-Value Work: 0.252 
  • R-Value Observed: 0.252 

wwPDB Validation   3D Report Full Report


This is version 1.3 of the entry. See complete history


Literature

The B-Box Dominates Sap-1/Srf Interactions in the Structure of the Ternary Complex

Hassler, M.Richmond, T.J.

(2001) EMBO J 20: 3018

  • DOI: https://doi.org/10.1093/emboj/20.12.3018
  • Primary Citation of Related Structures:  
    1HBX

  • PubMed Abstract: 

    The serum response element (SRE) is found in several immediate-early gene promoters. This DNA sequence is necessary and sufficient for rapid transcriptional induction of the human c-fos proto-oncogene in response to stimuli external to the cell. Full activation of the SRE requires the cooperative binding of a ternary complex factor (TCF) and serum response factor (SRF) to their specific DNA sites. The X-ray structure of the human SAP-1-SRF-SRE DNA ternary complex was determined (Protein Data Bank code 1hbx). It shows SAP-1 TCF bound to SRF through interactions between the SAP-1 B-box and SRF MADS domain in addition to contacts between their respective DNA-binding motifs. The SAP-1 B-box is part of a flexible linker of which 21 amino acids become ordered upon ternary complex formation. Comparison with a similar region from the yeast MATalpha2-MCM1-DNA complex suggests a common binding motif through which MADS-box proteins may interact with additional factors such as Fli-1.


  • Organizational Affiliation

    ETH Zürich, Institut für Molekularbiologie und Biophysik, ETH-Hönggerberg, CH-8093 Zürich, Switzerland.


Macromolecules

Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
SERUM RESPONSE FACTOR
A, B, D, E
92Homo sapiensMutation(s): 0 
Gene Names: SRF (132-223)
UniProt & NIH Common Fund Data Resources
Find proteins for P11831 (Homo sapiens)
Explore P11831 
Go to UniProtKB:  P11831
PHAROS:  P11831
GTEx:  ENSG00000112658 
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP11831
Sequence Annotations
Expand
  • Reference Sequence
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 3
MoleculeChains Sequence LengthOrganismDetailsImage
ETS-DOMAIN PROTEIN ELK-4
G, H
157Homo sapiensMutation(s): 0 
Gene Names: SAP-1 (1-156)
UniProt & NIH Common Fund Data Resources
Find proteins for P28324 (Homo sapiens)
Explore P28324 
Go to UniProtKB:  P28324
PHAROS:  P28324
GTEx:  ENSG00000158711 
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP28324
Sequence Annotations
Expand
  • Reference Sequence
Find similar nucleic acids by:  (by identity cutoff)  |  3D Structure
Entity ID: 2
MoleculeChains LengthOrganismImage
5'-D(*GP*AP*TP*GP*GP*CP*CP*TP*AP*AP*TP*TP*AP* GP*GP*AP*CP*TP*TP*CP*CP*GP*GP*TP*G)-3'
C, F
26Homo sapiens
Sequence Annotations
Expand
  • Reference Sequence
Find similar nucleic acids by:  (by identity cutoff)  |  3D Structure
Entity ID: 4
MoleculeChains LengthOrganismImage
5'-D(*CP*AP*CP*AP*CP*CP*GP*GP*AP*AP*GP*TP*CP* CP*TP*AP*AP*TP*TP*AP*GP*GP*CP*CP*AP*T)-3'I [auth W],
J [auth X]
26Homo sapiens
Sequence Annotations
Expand
  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 3.15 Å
  • R-Value Free: 0.285 
  • R-Value Work: 0.252 
  • R-Value Observed: 0.252 
  • Space Group: P 21 21 2
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 142.68α = 90
b = 144.39β = 90
c = 75.93γ = 90
Software Package:
Software NamePurpose
DENZOdata reduction
SCALEPACKdata scaling
AMoREphasing
CNSphasing
CNSrefinement

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2001-06-27
    Type: Initial release
  • Version 1.1: 2011-05-07
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance
  • Version 1.3: 2023-12-13
    Changes: Data collection, Database references, Other, Refinement description