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
- PubMed: 24056943 
- 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.