Unique Structural Fold of LonBA Protease from Bacillus subtilis, a Member of a Newly Identified Subfamily of Lon Proteases
In the study of ATP-dependent Lon proteases – key members of the cellular proteome quality control system, scientists from the Laboratory of Proteolytic Enzyme Chemistry of IBСh RAS in collaboration with colleagues from the National Cancer Institute (Frederick, USA) revealed a group of enzymes that bear structural features of participants of both previously studied basic LonA and LonB subfamilies. These enzymes were proposed to consider as a new "hybrid" LonBA subfamily. The protease (P) domain of LonBAs has a unique among Lon family fold as it was shown by 3D analysis of the enzyme from Bacillus subtilis (BsLonBA). The experimentally solved P domain structure was combined with the structure of the BsLonBA ATPase component modeled using the AlphaFold2 program. The predicted structure of full- length BsLonBA was compared with the known structures of LonA and LonB proteases. Possible peculiarities of the LonBA proteases functioning are discussed. The work was published in the International Journal of Molecular Sciences.
20 октября 2022 года