Title :

Conserved Omp85 lid-lock structure and substrate recognition in FhaC

Author(s) :

Maier, Timm [Auteur correspondant]
Université de Bâle = University of Basel = Basel Universität [Unibas]
Clantin, Bernard [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 [UGSF]
Gruss, Fabian [Auteur]
Université de Bâle = University of Basel = Basel Universität [Unibas]
Dewitte, Frederique [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 [UGSF]
Delattre, Anne-Sophie [Auteur]
Centre d’Infection et d’Immunité de Lille - INSERM U 1019 - UMR 9017 - UMR 8204 [CIIL]
Jacob-Dubuisson, Françoise [Auteur]
Centre d’Infection et d’Immunité de Lille - INSERM U 1019 - UMR 9017 - UMR 8204 [CIIL]
Hiller, Sebastian [Auteur correspondant]
Université de Bâle = University of Basel = Basel Universität [Unibas]
Villeret, Vincent [Auteur correspondant]
Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 [UGSF]

Journal title :

Nature Communications

Pages :

7452

Publisher :

Nature Publishing Group

Publication date :

2015-06-10

ISSN :

2041-1723

English keyword(s) :

Sequence Homology
Amino Acid
Amino Acid Sequence
Bacterial Outer Membrane Proteins
Escherichia coli Proteins
X-Ray Diffraction
Substrate Specificity
Molecular Sequence Data
Protein Conformation

HAL domain(s) :

Sciences du Vivant [q-bio]/Biochimie, Biologie Moléculaire/Biologie structurale [q-bio.BM]
Sciences du Vivant [q-bio]/Microbiologie et Parasitologie/Bactériologie

English abstract : [en]

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 ...
Show more >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.Show less >

Language :

Anglais

Popular science :

Non

ANR Project :

La Sécrétion à Deux Partenaires chez les bactéries : dynamique conformationnelle du transporteur FhaC.

Collections :

• Centre d'Infection et d'Immunité de Lille (CIIL) - U1019 - UMR 9017

Source :

Harvested from HAL