6AIT

Crystal structure of E. coli BepA

Summary for 6AIT

• Entry DOI: 10.2210/pdb6ait/pdb
• Descriptor: Beta-barrel assembly-enhancing protease, ZINC ION, 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL, ... (4 entities in total)
• Functional Keywords: hydrolase, metal binding protein
• Biological source: Escherichia coli (strain K12)
• Total number of polymer chains: 6
• Total formula weight: 294452.21

Authors

Umar, M.S.M.,Tanaka, Y.,Kamikubo, H.,Tsukazaki, T. (deposition date: 2018-08-24, release date: 2018-12-26, Last modification date: 2023-11-22)

Primary citation

Shahrizal, M.,Daimon, Y.,Tanaka, Y.,Hayashi, Y.,Nakayama, S.,Iwaki, S.,Narita, S.I.,Kamikubo, H.,Akiyama, Y.,Tsukazaki, T.
Structural Basis for the Function of the beta-Barrel Assembly-Enhancing Protease BepA.
J. Mol. Biol., 431:625-635, 2019

PubMed 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.

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

Experimental method

X-RAY DIFFRACTION (2.598 Å)