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 with sequence from Bordetella pertussis Tohama I. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.5Å Ligands: 1PE, BOG, P6G, PEG, PG4, PGE, PO4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT 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 Omp85 proteins mediate translocation of polypeptide substrates across and into cellular membranes. They share a common architecture comprising substrate-interacting POTRA domains, a C-terminal 16-stranded beta-barrel pore and two signature motifs located on the inner barrel wall and at the tip of the extended L6 loop. The observation of two distinct conformations of the L6 loop in the available Omp85 structures previously suggested a functional role of conformational changes in L6 in the Omp85 mechanism. Here we present a 2.5 A resolution structure of a variant of the Omp85 secretion protein FhaC, in which the two signature motifs interact tightly and form the conserved 'lid lock'. Reanalysis of previous structural data shows that L6 adopts the same, conserved resting state position in all available Omp85 structures. The FhaC variant structure further reveals a competitive mechanism for the regulation of substrate binding mediated by the linker to the N-terminal plug helix H1. Conserved Omp85 lid-lock structure and substrate recognition in FhaC.,Maier T, Clantin B, Gruss F, Dewitte F, Delattre AS, Jacob-Dubuisson F, Hiller S, Villeret V Nat Commun. 2015 Jun 10;6:7452. doi: 10.1038/ncomms8452. PMID:26058369 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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