Conserved Omp85 lid-lock structure and substrate recognition in FhaC - Université de Lille Accéder directement au contenu
Article Dans Une Revue Nature Communications Année : 2015

Conserved Omp85 lid-lock structure and substrate recognition in FhaC


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.
Fichier principal
Vignette du fichier
ncomms8452.pdf (2.15 Mo) Télécharger le fichier
Origine Fichiers éditeurs autorisés sur une archive ouverte

Dates et versions

hal-03182009 , version 1 (26-03-2021)




Timm Maier, Bernard Clantin, Fabian Gruss, Frederique Dewitte, Anne-Sophie Delattre, et al.. Conserved Omp85 lid-lock structure and substrate recognition in FhaC. Nature Communications, 2015, 6, pp.7452. ⟨10.1038/ncomms8452⟩. ⟨hal-03182009⟩
41 Consultations
49 Téléchargements



Gmail Mastodon Facebook X LinkedIn More