4ql0 | pdb_00004ql0

Crystal Structure Analysis of the Membrane Transporter FhaC (double mutant V169T, I176N)

spinqualitylabelsall models 4ql0, resolution 2.50Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4ql0 is a 1 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: 1PE, BOG, P6G, PEG, PG4, PGE, PO4 Related: 4qky, 2qdz Resources: FirstGlance, OCA, RCSB, PDBsum Function [FHAC_BORPE] Member of a two partner secretion pathway (TPS) in which it mediates the secretion of filamentous hemagglutinin (FHA). 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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