Structural highlights
Function
[FHAC_BORPE] Member of a two partner secretion pathway (TPS) in which it mediates the secretion of filamentous hemagglutinin (FHA).[1]
Publication Abstract from PubMed
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.
Structure of the membrane protein FhaC: a member of the Omp85-TpsB transporter superfamily.,Clantin B, Delattre AS, Rucktooa P, Saint N, Meli AC, Locht C, Jacob-Dubuisson F, Villeret V Science. 2007 Aug 17;317(5840):957-61. PMID:17702945[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Hodak H, Clantin B, Willery E, Villeret V, Locht C, Jacob-Dubuisson F. Secretion signal of the filamentous haemagglutinin, a model two-partner secretion substrate. Mol Microbiol. 2006 Jul;61(2):368-82. Epub 2006 Jun 12. PMID:16771844 doi:10.1111/j.1365-2958.2006.05242.x
- ↑ Clantin B, Delattre AS, Rucktooa P, Saint N, Meli AC, Locht C, Jacob-Dubuisson F, Villeret V. Structure of the membrane protein FhaC: a member of the Omp85-TpsB transporter superfamily. Science. 2007 Aug 17;317(5840):957-61. PMID:17702945 doi:317/5840/957
