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Publication Abstract from PubMed

The beta-barrel assembly machinery (BAM) complex mediates the assembly of beta-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 beta-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-A 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.

Structural Basis for the Function of the beta-Barrel Assembly-Enhancing Protease BepA.,Shahrizal M, Daimon Y, Tanaka Y, Hayashi Y, Nakayama S, Iwaki S, Narita SI, Kamikubo H, Akiyama Y, Tsukazaki T J Mol Biol. 2018 Dec 3. pii: S0022-2836(18)31008-8. doi:, 10.1016/j.jmb.2018.11.024. PMID:30521812^[3]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.