2WQ1

GCN4 leucine zipper mutant with three IxxNTxx motifs coordinating bromide


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.08 Å
  • R-Value Free: 0.167 
  • R-Value Work: 0.127 
  • R-Value Observed: 0.129 

wwPDB Validation   3D Report Full Report


This is version 1.2 of the entry. See complete history


Literature

A Coiled-Coil Motif that Sequesters Ions to the Hydrophobic Core.

Hartmann, M.D.Ridderbusch, O.Zeth, K.Albrecht, R.Testa, O.Woolfson, D.N.Sauer, G.Dunin-Horkawicz, S.Lupas, A.N.Alvarez, B.H.

(2009) Proc Natl Acad Sci U S A 106: 16950

  • DOI: https://doi.org/10.1073/pnas.0907256106
  • Primary Citation of Related Structures:  
    2WPQ, 2WPR, 2WPS, 2WPY, 2WPZ, 2WQ0, 2WQ1, 2WQ2, 2WQ3

  • PubMed Abstract: 

    Most core residues of coiled coils are hydrophobic. Occasional polar residues are thought to lower stability, but impart structural specificity. The coiled coils of trimeric autotransporter adhesins (TAAs) are conspicuous for their large number of polar residues in position d of the core, which often leads to their prediction as natively unstructured regions. The most frequent residue, asparagine (N@d), can occur in runs of up to 19 consecutive heptads, frequently in the motif [I/V]xxNTxx. In the Salmonella TAA, SadA, the core asparagines form rings of interacting residues with the following threonines, grouped around a central anion. This conformation is observed generally in N@d layers from trimeric coiled coils of known structure. Attempts to impose a different register on the motif show that the asparagines orient themselves specifically into the core, even against conflicting information from flanking domains. When engineered into the GCN4 leucine zipper, N@d layers progressively destabilized the structure, but zippers with 3 N@d layers still folded at high concentration. We propose that N@d layers maintain the coiled coils of TAAs in a soluble, export-competent state during autotransport through the outer membrane. More generally, we think that polar motifs that are both periodic and conserved may often reflect special folding requirements, rather than an unstructured state of the mature proteins.


  • Organizational Affiliation

    Department of Protein Evolution, Max Planck Institute for Developmental Biology, 72076 Tübingen, Germany.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
GENERAL CONTROL PROTEIN GCN433Saccharomyces cerevisiaeMutation(s): 9 
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
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.08 Å
  • R-Value Free: 0.167 
  • R-Value Work: 0.127 
  • R-Value Observed: 0.129 
  • Space Group: I 21 3
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 56.58α = 90
b = 56.58β = 90
c = 56.58γ = 90
Software Package:
Software NamePurpose
REFMACrefinement
XDSdata reduction
XSCALEdata scaling
SHELXphasing

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2009-11-03
    Type: Initial release
  • Version 1.1: 2011-05-08
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance