4C46

ANDREI-N-LVPAS fused to GCN4 adaptors


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.95 Å
  • R-Value Free: 0.275 
  • R-Value Work: 0.238 
  • R-Value Observed: 0.240 

wwPDB Validation   3D Report Full Report


This is version 1.5 of the entry. See complete history


Literature

Your Personalized Protein Structure: Andrei N. Lupas Fused to GCN4 Adaptors.

Deiss, S.Hernandez Alvarez, B.Bar, K.Ewers, C.P.Coles, M.Albrecht, R.Hartmann, M.D.

(2014) J Struct Biol 186: 380

  • DOI: https://doi.org/10.1016/j.jsb.2014.01.013
  • Primary Citation of Related Structures:  
    4C46

  • PubMed Abstract: 

    This work presents a protein structure that has been designed purely for aesthetic reasons, symbolizing decades of coiled-coil research and praising its most fundamental model system, the GCN4 leucine zipper. The GCN4 leucine zipper is a highly stable coiled coil which can be tuned to adopt different oligomeric states via mutation of its core residues. For these reasons it is used in structural studies as a stabilizing fusion adaptor. On the occasion of the 50th birthday of Andrei N. Lupas, we used it to create the first personalized protein structure: we fused the sequence ANDREI-N-LVPAS in heptad register to trimeric GCN4 adaptors and determined its structure by X-ray crystallography. The structure demonstrates the robustness and versatility of GCN4 as a fusion adaptor. We learn how proline can be accommodated in trimeric coiled coils, and put the structure into the context of the other GCN4-fusion structures known to date.


  • Organizational Affiliation

    Department of Protein Evolution, Max Planck Institute for Developmental Biology, Spemannstraße 35, D-72076 Tübingen, Germany.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
GENERAL CONTROL PROTEIN GCN4, GENERAL CONTROL PROTEIN GCN4
A, B, C
76Saccharomyces cerevisiaeMutation(s): 18 
UniProt
Find proteins for P03069 (Saccharomyces cerevisiae (strain ATCC 204508 / S288c))
Explore P03069 
Go to UniProtKB:  P03069
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP03069
Sequence Annotations
Expand
  • Reference Sequence
Small Molecules
Ligands 1 Unique
IDChains Name / Formula / InChI Key2D Diagram3D Interactions
BR
Query on BR

Download Ideal Coordinates CCD File 
D [auth A]BROMIDE ION
Br
CPELXLSAUQHCOX-UHFFFAOYSA-M
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.95 Å
  • R-Value Free: 0.275 
  • R-Value Work: 0.238 
  • R-Value Observed: 0.240 
  • Space Group: P 1 21 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 42α = 90
b = 41.6β = 95.48
c = 64.14γ = 90
Software Package:
Software NamePurpose
REFMACrefinement
XDSdata reduction
XDSdata scaling
MOLREPphasing

Structure Validation

View Full Validation Report



Entry History 

Revision History  (Full details and data files)

  • Version 1.0: 2013-09-11
    Type: Initial release
  • Version 1.1: 2014-01-29
    Changes: Database references, Structure summary
  • Version 1.2: 2014-03-19
    Changes: Database references
  • Version 1.3: 2014-06-11
    Changes: Database references
  • Version 1.4: 2019-05-08
    Changes: Data collection, Experimental preparation, Other
  • Version 1.5: 2023-12-20
    Changes: Data collection, Database references, Derived calculations, Other, Refinement description