4C47

Salmonella enterica trimeric lipoprotein SadB


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.45 Å
  • R-Value Free: 0.242 
  • R-Value Work: 0.204 
  • R-Value Observed: 0.206 

wwPDB Validation   3D Report Full Report


This is version 1.3 of the entry. See complete history


Literature

A Trimeric Lipoprotein Assists in Trimeric Autotransporter Biogenesis in Enterobacteria.

Grin, I.Hartmann, M.D.Sauer, G.Hernandez Alvarez, B.Schutz, M.Madlung, J.Macek, B.Felipe-Lopez, A.Hensel, M.Lupas, A.Linke, D.

(2014) J Biol Chem 289: 7388

  • DOI: https://doi.org/10.1074/jbc.M113.513275
  • Primary Citation of Related Structures:  
    4C47

  • PubMed Abstract: 

    Trimeric autotransporter adhesins (TAAs) are important virulence factors of many Gram-negative bacterial pathogens. TAAs form fibrous, adhesive structures on the bacterial cell surface. Their N-terminal extracellular domains are exported through a C-terminal membrane pore; the insertion of the pore domain into the bacterial outer membrane follows the rules of β-barrel transmembrane protein biogenesis and is dependent on the essential Bam complex. We have recently described the full fiber structure of SadA, a TAA of unknown function in Salmonella and other enterobacteria. In this work, we describe the structure and function of SadB, a small inner membrane lipoprotein. The sadB gene is located in an operon with sadA; orthologous operons are only found in enterobacteria, whereas other TAAs are not typically associated with lipoproteins. Strikingly, SadB is also a trimer, and its co-expression with SadA has a direct influence on SadA structural integrity. This is the first report of a specific export factor of a TAA, suggesting that at least in some cases TAA autotransport is assisted by additional periplasmic proteins.


  • Organizational Affiliation

    From the Max Planck Institut für Entwicklungsbiologie, 72076 Tübingen.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
INNER MEMBRANE LIPOPROTEIN
A, B, C
207Salmonella enterica subsp. enterica serovar Typhimurium str. LT2Mutation(s): 0 
UniProt
Find proteins for Q8ZL65 (Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720))
Explore Q8ZL65 
Go to UniProtKB:  Q8ZL65
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ8ZL65
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.45 Å
  • R-Value Free: 0.242 
  • R-Value Work: 0.204 
  • R-Value Observed: 0.206 
  • Space Group: H 3
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 118.45α = 90
b = 118.45β = 90
c = 159.18γ = 120
Software Package:
Software NamePurpose
PHENIXrefinement
XDSdata reduction
XDSdata scaling
SHELXphasing

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2014-01-08
    Type: Initial release
  • Version 1.1: 2014-01-15
    Changes: Database references
  • Version 1.2: 2014-04-02
    Changes: Database references
  • Version 1.3: 2019-05-08
    Changes: Data collection, Experimental preparation, Other