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J Mol Biol. 2019 Feb 1;431(3):625-635. doi: 10.1016/j.jmb.2018.11.024. Epub 2018 Dec 3.

Structural Basis for the Function of the β-Barrel Assembly-Enhancing Protease BepA.

Author information

1
Nara Institute of Science and Technology, Ikoma, Nara 630-0192, Japan.
2
Institute for Frontier Life and Medical Sciences, Kyoto University, Kyoto 606-8507, Japan.
3
Faculty of Nutritional Sciences, University of Morioka, Iwate 020-0694, Japan.
4
Institute for Frontier Life and Medical Sciences, Kyoto University, Kyoto 606-8507, Japan. Electronic address: yakiyama@infront.kyoto-u.ac.jp.
5
Nara Institute of Science and Technology, Ikoma, Nara 630-0192, Japan. Electronic address: ttsukazaki@mac.com.

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.

KEYWORDS:

chaperon; crystal structure; outer membrane; protease; protein biogenesis

PMID:
30521812
DOI:
10.1016/j.jmb.2018.11.024

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