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Structural Basis for the Function of the β-Barrel Assembly-Enhancing Protease BepA.
- Source :
-
Journal of Molecular Biology . Feb2019, Vol. 431 Issue 3, p625-635. 11p. - Publication Year :
- 2019
-
Abstract
- Abstract The β-barrel assembly machinery (BAM) complex mediates the assembly of β-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 β-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. Graphical Abstract Unlabelled Image Highlights • Crystal structure (2.6 Å) of full-length BepA, β-barrel assembly-enhancing protease BepA • Crystal structure represents both its functional and resting states. • Functional model of BepA was proposed. [ABSTRACT FROM AUTHOR]
- Subjects :
- *PROTEOLYTIC enzymes
*PROTEINS
*BIOSYNTHESIS
*PROTEIN tags
*CRYSTAL structure
Subjects
Details
- Language :
- English
- ISSN :
- 00222836
- Volume :
- 431
- Issue :
- 3
- Database :
- Academic Search Index
- Journal :
- Journal of Molecular Biology
- Publication Type :
- Academic Journal
- Accession number :
- 134275364
- Full Text :
- https://doi.org/10.1016/j.jmb.2018.11.024