Structure and function of BamE within the outer membrane and the ß-barrel assembly machine.
EMBO Rep
; 12(2): 123-8, 2011 Feb.
Article
en En
| MEDLINE
| ID: mdl-21212804
ABSTRACT
Insertion of folded proteins into the outer membrane of Gram-negative bacteria is mediated by the essential ß-barrel assembly machine (Bam). Here, we report the native structure and mechanism of a core component of this complex, BamE, and show that it is exclusively monomeric in its native environment of the periplasm, but is able to adopt a distinct dimeric conformation in the cytoplasm. BamE is shown to bind specifically to phosphatidylglycerol, and comprehensive mutagenesis and interaction studies have mapped key determinants for complex binding, outer membrane integrity and cell viability, as well as revealing the role of BamE within the Bam complex.
Texto completo:
1
Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Conformación Proteica
/
Proteínas de la Membrana Bacteriana Externa
/
Proteínas de Escherichia coli
/
Proteínas Mutantes
Idioma:
En
Revista:
EMBO Rep
Asunto de la revista:
BIOLOGIA MOLECULAR
Año:
2011
Tipo del documento:
Article
País de afiliación:
Reino Unido