Structural Basis for the Function of the ß-Barrel Assembly-Enhancing Protease BepA.
J Mol Biol
; 431(3): 625-635, 2019 02 01.
Article
em En
| MEDLINE
| ID: mdl-30521812
ABSTRACT
The ß-barrel assembly machinery (BAM) complex mediates the assembly of ß-barrel membrane proteins in the outer membrane. BepA, formerly known as YfgC, interacts with the BAM complex and functions as a protease/chaperone for the enhancement of the assembly and/or degradation of ß-barrel membrane proteins. To elucidate the molecular mechanism underlying the dual functions of BepA, its full-length three-dimensional structure is needed. Here, we report the crystal structure of full-length BepA at 2.6-Å resolution. BepA possesses an N-terminal protease domain and a C-terminal tetratricopeptide repeat domain, which interact with each other. Domain cross-linking by structure-guided introduction of disulfide bonds did not affect the activities of BepA in vivo, suggesting that the function of this protein does not involve domain rearrangement. The full-length BepA structure is compatible with the previously proposed docking model of BAM complex and tetratricopeptide repeat domain of BepA.
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Texto completo:
1
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Proteínas da Membrana Bacteriana Externa
/
Proteínas de Escherichia coli
/
Metaloproteases
Idioma:
En
Revista:
J Mol Biol
Ano de publicação:
2019
Tipo de documento:
Article
País de afiliação:
Japão