Conserved Omp85 lid-lock structure and ...
Type de document :
Article dans une revue scientifique
DOI :
PMID :
URL permanente :
Titre :
Conserved Omp85 lid-lock structure and substrate recognition in FhaC
Auteur(s) :
Maier, Timm [Auteur]
Clantin, Bernard [Auteur]
Gruss, Fabian [Auteur]
Dewitte, Frederique [Auteur]
Delattre, Anne-Sophie [Auteur]
Jacob-Dubuisson, Françoise [Auteur]
Hiller, Sebastian [Auteur]
Villeret, Vincent [Auteur]
Clantin, Bernard [Auteur]
Gruss, Fabian [Auteur]
Dewitte, Frederique [Auteur]
Delattre, Anne-Sophie [Auteur]
Jacob-Dubuisson, Françoise [Auteur]
Hiller, Sebastian [Auteur]
Villeret, Vincent [Auteur]
Titre de la revue :
Nature communications
Nom court de la revue :
Nat Commun
Numéro :
6
Pagination :
7452
Date de publication :
2015-06-10
ISSN :
2041-1723
Mot(s)-clé(s) en anglais :
Sequence Homology, Amino Acid
Amino Acid Sequence
Bacterial Outer Membrane Proteins
Escherichia coli Proteins
X-Ray Diffraction
Substrate Specificity
Molecular Sequence Data
Protein Conformation
Amino Acid Sequence
Bacterial Outer Membrane Proteins
Escherichia coli Proteins
X-Ray Diffraction
Substrate Specificity
Molecular Sequence Data
Protein Conformation
Discipline(s) HAL :
Chimie/Chimie théorique et/ou physique
Résumé en anglais : [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 ...
Lire la suite >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.Lire moins >
Lire la suite >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.Lire moins >
Langue :
Anglais
Établissement(s) :
CNRS
Université de Lille
Université de Lille
Équipe(s) de recherche :
Biologie structurale et intégrative
Date de dépôt :
2020-02-12T15:11:31Z