4QKY

Crystal Structure Analysis of the Membrane Transporter FhaC

Replaces:  2QDZ

Summary for 4QKY

• Entry DOI: 10.2210/pdb4qky/pdb
• Related: 2QDZ 4QL0
• Descriptor: Filamentous hemagglutinin transporter protein FhaC, PHOSPHATE ION (2 entities in total)
• Functional Keywords: beta barrel, potra domain, protein transport, outer membrane
• Biological source: Bordetella pertussis
• Cellular location: Cell outer membrane : P35077
• Total number of polymer chains: 1
• Total formula weight: 61507.81

Authors

Maier, T.,Clantin, B.,Gruss, F.,Dewitte, F.,Delattre, A.S.,Jacob-Dubuisson, F.,Hiller, S.,Villeret, V. (deposition date: 2014-06-10, release date: 2014-10-22, Last modification date: 2024-03-20)

Primary citation

Maier, T.,Clantin, B.,Gruss, F.,Dewitte, F.,Delattre, A.S.,Jacob-Dubuisson, F.,Hiller, S.,Villeret, V.
Conserved Omp85 lid-lock structure and substrate recognition in FhaC
Nat Commun, 6:7452-7452, 2015

PubMed Abstract: 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 β-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 Å 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.

PubMed: 26058369
DOI: 10.1038/ncomms8452

Experimental method

X-RAY DIFFRACTION (2.9 Å)