1. Structure of the Membrane Protein FhaC: A Member of the Omp85-TpsB Transporter Superfamily.
- Author
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Clantin, Bernard, Detattre, Anne-Sophie, Rucktooa, Prakash, Saint, Nathalie, Méli, Albano C., Locht, Camille, Jacob-Dubuisson, Françoise, and Villeret, Vincent
- Subjects
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MEMBRANE proteins , *GRAM-negative bacteria , *BORDETELLA pertussis , *CELL membranes , *CHROMOSOMAL translocation , *PROTEIN-protein interactions - Abstract
In Gram-negative bacteria and eukaryotic organelles, β-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 β barrel that is occluded by an N-terminal a 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. [ABSTRACT FROM AUTHOR]
- Published
- 2007
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