6ait
From Proteopedia
Crystal structure of E. coli BepA
Structural highlights
FunctionBEPA_ECOLI Functions as both a chaperone and a metalloprotease. Maintains the integrity of the outer membrane by promoting either the assembly or the elimination of outer membrane proteins, depending on their folding state. Promotes disulfide rearrangement of LptD during its biogenesis, and proteolytic degradation of LptD and BamA when their proper assembly is compromised. May facilitate membrane attachment of LoiP under unfavorable conditions.[HAMAP-Rule:MF_00997][1] [2] Publication Abstract from PubMedThe 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. References
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