2QA5

Crystal structure of Sept2 G-domain


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 3.40 Å
  • R-Value Free: 0.314 
  • R-Value Work: 0.280 
  • R-Value Observed: 0.281 

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This is version 1.1 of the entry. See complete history


Literature

Structural insight into filament formation by mammalian septins.

Sirajuddin, M.Farkasovsky, M.Hauer, F.Kuhlmann, D.Macara, I.G.Weyand, M.Stark, H.Wittinghofer, A.

(2007) Nature 449: 311-315

  • DOI: https://doi.org/10.1038/nature06052
  • Primary Citation of Related Structures:  
    2QA5, 2QAG

  • PubMed Abstract: 

    Septins are GTP-binding proteins that assemble into homo- and hetero-oligomers and filaments. Although they have key roles in various cellular processes, little is known concerning the structure of septin subunits or the organization and polarity of septin complexes. Here we present the structures of the human SEPT2 G domain and the heterotrimeric human SEPT2-SEPT6-SEPT7 complex. The structures reveal a universal bipolar polymer building block, composed of an extended G domain, which forms oligomers and filaments by conserved interactions between adjacent nucleotide-binding sites and/or the amino- and carboxy-terminal extensions. Unexpectedly, X-ray crystallography and electron microscopy showed that the predicted coiled coils are not involved in or required for complex and/or filament formation. The asymmetrical heterotrimers associate head-to-head to form a hexameric unit that is nonpolarized along the filament axis but is rotationally asymmetrical. The architecture of septin filaments differs fundamentally from that of other cytoskeletal structures.


  • Organizational Affiliation

    Abteilung Strukturelle Biologie, Max-Planck-Institut für molekulare Physiologie, Otto-Hahn-Strasse 11, 44227 Dortmund, Germany.


Macromolecules
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Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Septin-2
A, B
315Homo sapiensMutation(s): 0 
Gene Names: SEPT2DIFF6KIAA0158NEDD5
UniProt & NIH Common Fund Data Resources
Find proteins for Q15019 (Homo sapiens)
Explore Q15019 
Go to UniProtKB:  Q15019
PHAROS:  Q15019
GTEx:  ENSG00000168385 
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ15019
Sequence Annotations
Expand
  • Reference Sequence
Small Molecules
Modified Residues  1 Unique
IDChains TypeFormula2D DiagramParent
MSE
Query on MSE
A, B
L-PEPTIDE LINKINGC5 H11 N O2 SeMET
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 3.40 Å
  • R-Value Free: 0.314 
  • R-Value Work: 0.280 
  • R-Value Observed: 0.281 
  • Space Group: C 1 2 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 162.96α = 90
b = 53.92β = 128.37
c = 110.27γ = 90
Software Package:
Software NamePurpose
REFMACrefinement
PDB_EXTRACTdata extraction

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2007-08-07
    Type: Initial release
  • Version 1.1: 2011-07-13
    Changes: Version format compliance