Structure of the membrane protein FhaC: a member of the Omp85-TpsB transporter superfamily |
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| Authors: | Clantin Bernard Delattre Anne-Sophie Rucktooa Prakash Saint Nathalie Méli Albano C Locht Camille Jacob-Dubuisson Françoise Villeret Vincent |
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| Institution: | 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. |
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| Abstract: | In Gram-negative bacteria and eukaryotic organelles, beta-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 A crystal structure of FhaC. The transporter comprises a 16-stranded beta 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. |
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