4BZA

Crystal structure of TamA POTRA domains 1-3 from E. coli


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.84 Å
  • R-Value Free: 0.202 
  • R-Value Work: 0.173 
  • R-Value Observed: 0.174 

wwPDB Validation   3D Report Full Report


This is version 1.3 of the entry. See complete history


Literature

The Structural Basis of Autotransporter Translocation by Tama

Gruss, F.Zaehringer, F.Jakob, R.P.Burmann, B.M.Hiller, S.Maier, T.

(2013) Nat Struct Mol Biol 20: 1318

  • DOI: https://doi.org/10.1038/nsmb.2689
  • Primary Citation of Related Structures:  
    4BZA, 4C00

  • PubMed Abstract: 

    TamA is an Escherichia coli Omp85 protein involved in autotransporter biogenesis. It comprises a 16-stranded transmembrane β-barrel and three POTRA domains. The 2.3-Å crystal structure reveals that the TamA barrel is closed at the extracellular face by a conserved lid loop. The C-terminal β-strand of the barrel forms an unusual inward kink, which weakens the lateral barrel wall and creates a gate for substrate access to the lipid bilayer.


  • Organizational Affiliation

    Biozentrum, University of Basel, Basel, Switzerland.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
TRANSLOCATION AND ASSEMBLY MODULE TAMA261Escherichia coli BL21(DE3)Mutation(s): 0 
Membrane Entity: Yes 
UniProt
Find proteins for P0ADE4 (Escherichia coli (strain K12))
Explore P0ADE4 
Go to UniProtKB:  P0ADE4
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP0ADE4
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.84 Å
  • R-Value Free: 0.202 
  • R-Value Work: 0.173 
  • R-Value Observed: 0.174 
  • Space Group: P 43 21 2
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 83.05α = 90
b = 83.05β = 90
c = 150.66γ = 90
Software Package:
Software NamePurpose
XDSdata reduction
XDSdata scaling
SHELXphasing
PHASERphasing
PHENIXrefinement

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2013-09-25
    Type: Initial release
  • Version 1.1: 2013-10-02
    Changes: Database references
  • Version 1.2: 2013-11-20
    Changes: Database references
  • Version 1.3: 2024-05-08
    Changes: Data collection, Database references, Derived calculations, Other