Laboratory of Microbial Cell Surface Biochemistry, G.K. Skryabin Institute of Biochemistry and Physiology of Microorganisms, FRC PSCBR, Russian Academy of Sciences, 5 Prosp. Nauki, 142290 Pushchino, Russia.
Institute of Protein Research, Russian Academy of Sciences, 4 Institutskaya Str., 142290 Pushchino, Russia.
Int J Mol Sci. 2022 Dec 17;23(24):16100. doi: 10.3390/ijms232416100.
The crystal structure of the VKM B-2533 β-lytic protease (Blp), a medicinally promising antimicrobial enzyme, was first solved. Blp was established to possess a folding characteristic of the M23 protease family. The groove of the Blp active site, as compared with that of the LasA structural homologue from , was found to have amino acid differences. Biochemical analysis revealed no differences in the optimal reaction conditions for manifesting Blp and LasA bacteriolytic activities. At the same time, Blp had a broader range of action against living and autoclaved target cells. The results suggest that the distinction in the geometry of the active site and the charge of amino acid residues that form the active site groove can be important for the hydrolysis of different peptidoglycan types in target cells.
首次解析了 VKM B-2533β-溶菌酶（Blp）的晶体结构，这是一种具有医学应用前景的抗菌酶。Blp 被确定具有 M23 蛋白酶家族的折叠特征。与来自 的 LasA 结构同源物相比，Blp 活性位点的凹槽被发现具有氨基酸差异。生化分析表明，表现 Blp 和 LasA 溶菌活性的最佳反应条件没有差异。同时，Blp 对活细胞和巴氏消毒的靶细胞具有更广泛的作用范围。研究结果表明，活性位点的几何形状和形成活性位点凹槽的氨基酸残基的电荷差异可能对靶细胞中不同肽聚糖类型的水解很重要。
