2qdz | pdb_00002qdz
Structure of the membrane protein fhac: a member of the omp85/tpsb transporter family
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Overview
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.
About this Structure
2QDZ is a Single protein structure of sequence from Bordetella pertussis. Full crystallographic information is available from OCA.
Reference
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
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