Structural insight into the formation of lipoprotein-ß-barrel complexes.
Nat Chem Biol
; 16(9): 1019-1025, 2020 09.
Article
en En
| MEDLINE
| ID: mdl-32572278
ABSTRACT
The ß-barrel assembly machinery (BAM) inserts outer membrane ß-barrel proteins (OMPs) in the outer membrane of Gram-negative bacteria. In Enterobacteriacea, BAM also mediates export of the stress sensor lipoprotein RcsF to the cell surface by assembling RcsF-OMP complexes. Here, we report the crystal structure of the key BAM component BamA in complex with RcsF. BamA adopts an inward-open conformation, with the lateral gate to the membrane closed. RcsF is lodged deep within the lumen of the BamA barrel, binding regions proposed to undergo outward and lateral opening during OMP insertion. On the basis of our structural and biochemical data, we propose a push-and-pull model for RcsF export following conformational cycling of BamA, and provide a mechanistic explanation for how RcsF uses its interaction with BamA to detect envelope stress. Our data also suggest that the flux of incoming OMP substrates is involved in the control of BAM activity.
Texto completo:
1
Banco de datos:
MEDLINE
Asunto principal:
Proteínas de la Membrana Bacteriana Externa
/
Proteínas de Escherichia coli
/
Escherichia coli
Idioma:
En
Revista:
Nat Chem Biol
Asunto de la revista:
BIOLOGIA
/
QUIMICA
Año:
2020
Tipo del documento:
Article
País de afiliación:
Bélgica