Structural highlights
Publication Abstract from PubMed
The crystal structure of the Lysobacter capsici VKM B-2533(T) beta-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 Pseudomonas aeruginosa, 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.
Structural and Functional Characterization of beta-lytic Protease from Lysobacter capsici VKM B-2533(T).,Afoshin A, Tishchenko S, Gabdulkhakov A, Kudryakova I, Galemina I, Zelenov D, Leontyevskaya E, Saharova S, Leontyevskaya Vasilyeva N Int J Mol Sci. 2022 Dec 17;23(24):16100. doi: 10.3390/ijms232416100. PMID:36555752[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Afoshin A, Tishchenko S, Gabdulkhakov A, Kudryakova I, Galemina I, Zelenov D, Leontyevskaya E, Saharova S, Leontyevskaya Vasilyeva N. Structural and Functional Characterization of β-lytic Protease from Lysobacter capsici VKM B-2533(T). Int J Mol Sci. 2022 Dec 17;23(24):16100. PMID:36555752 doi:10.3390/ijms232416100
