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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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THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
Omp85Tt from Thermus thermophilus HB27: an Ancestral Type of the Omp85 Protein Family.
J. Nesper, A. Brosig, P. Ringler, G. J. Patel, S. A. Muller, J. H. Kleinschmidt, W. Boos, K. Diederichs, and W. Welte (2008)
J. Bacteriol. 190, 4568-4575
   Abstract »    Full Text »    PDF »
The TpsB Translocator HMW1B of Haemophilus influenzae Forms a Large Conductance Channel.
G. Duret, M. Szymanski, K.-J. Choi, H.-J. Yeo, and A. H. Delcour (2008)
J. Biol. Chem. 283, 15771-15778
   Abstract »    Full Text »    PDF »


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Science. ISSN 0036-8075 (print), 1095-9203 (online)