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The structural basis of autotransporter translocation by TamA


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.

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Figure 1: TamA structure and interactions of its POTRA domains.
Figure 2: The closed lid and the lateral gate of TamA.
Figure 3: Proposed mechanism for substrate assembly through hybrid-barrel formation.

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Crystallographic experiments were performed at PXIII (Swiss Light Source, Paul Scherrer Institute, Switzerland). We thank M. Wang and V. Olieric for support at the beamline, T. Schirmer for discussion and L. Betancor and P.F. Leadlay (University of Cambridge) for the pL1SL2 plasmid. This work was supported by the Swiss National Science Foundation (Grant PP00P3_128419 to S.H.) and the European Research Council (FP7 contract MOMP 281764 to S.H.). F.G. acknowledges a fellowship by the Werner-Siemens Foundation.

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Authors and Affiliations



S.H. and T.M. designed the study and guided the research experiments. F.G., F.Z., R.P.J. and B.M.B. carried out the experiments. All authors analyzed data. F.G., S.H. and T.M. wrote the paper.

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Correspondence to Sebastian Hiller or Timm Maier.

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The authors declare no competing financial interests.

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Supplementary Figures 1–4 and Supplementary Table 1 (PDF 2325 kb)

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Gruss, F., Zähringer, F., Jakob, R. et al. The structural basis of autotransporter translocation by TamA. Nat Struct Mol Biol 20, 1318–1320 (2013).

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