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Science 17 August 2007:
Vol. 317. no. 5840, pp. 957 - 961
DOI: 10.1126/science.1143860
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Reports

Structure of the Membrane Protein FhaC: A Member of the Omp85-TpsB Transporter Superfamily

Bernard Clantin,1,2,3 Anne-Sophie Delattre,2,3,4 Prakash Rucktooa,1,2,3 Nathalie Saint,5,6 Albano C. Méli,5,6 Camille Locht,2,3,4 Françoise Jacob-Dubuisson,2,3,4* Vincent Villeret1,2,3*

In Gram-negative bacteria and eukaryotic organelles, ß-barrel proteins of the outer membrane protein 85–two-partner secretion B (Omp85-TpsB) superfamily are essential components of protein transport machineries. The TpsB transporter FhaC mediates the secretion of Bordetella pertussis filamentous hemagglutinin (FHA). We report the 3.15 Å crystal structure of FhaC. The transporter comprises a 16-stranded ß barrel that is occluded by an N-terminal {alpha} helix and an extracellular loop and a periplasmic module composed of two aligned polypeptide-transport–associated (POTRA) domains. Functional data reveal that FHA binds to the POTRA 1 domain via its N-terminal domain and likely translocates the adhesin-repeated motifs in an extended hairpin conformation, with folding occurring at the cell surface. General features of the mechanism obtained here are likely to apply throughout the superfamily.

1 UMR8161 CNRS, Institut de Biologie de Lille, Université de Lille 1, Université de Lille 2, 1 rue du Prof. Calmette, F-59021 Lille cedex, France.
2 Institut Pasteur de Lille, Lille, 1 rue du Prof. Calmette, F-59019 Lille cedex, France.
3 IFR142, 59019 Lille, France.
4 INSERM, U629, 59019 Lille, France.
5 INSERM, U554, 34090 Montpellier, France.
6 UMR5048 CNRS, Université de Montpellier 1, Université de Montpellier 2, Montpellier, France.

* To whom correspondence should be addressed. E-mail: francoise.jacob{at}ibl.fr (F.J.-D.); vincent.villeret{at}ibl.fr (V.V.)

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