1. Structural Basis for the Function of the β-Barrel Assembly-Enhancing Protease BepA.
- Author
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Shahrizal M, Daimon Y, Tanaka Y, Hayashi Y, Nakayama S, Iwaki S, Narita SI, Kamikubo H, Akiyama Y, and Tsukazaki T
- Subjects
- Crystallography, X-Ray methods, Escherichia coli chemistry, Models, Molecular, Protein Domains, Protein Folding, Bacterial Outer Membrane Proteins chemistry, Escherichia coli Proteins chemistry, Metalloproteases chemistry
- 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., (Copyright © 2018 Elsevier Ltd. All rights reserved.)
- Published
- 2019
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