8AF1
Beta-Lytic Protease from Lysobacter capsici
Summary for 8AF1
| Entry DOI | 10.2210/pdb8af1/pdb |
| Descriptor | Peptidase M23, ZINC ION, CHLORIDE ION, ... (6 entities in total) |
| Functional Keywords | elastase, peptidoglycan, hydrolase, beta-lytic protease; antimicrobial activity; lysobacter, metalloprotease |
| Biological source | Lysobacter capsici |
| Total number of polymer chains | 1 |
| Total formula weight | 19552.92 |
| Authors | Gabdulkhakov, A.G.,Tishchenko, T.V.,Kudryakova, I.V.,Afoshin, A.S.,Vasilyeva, N.V. (deposition date: 2022-07-15, release date: 2023-08-16, Last modification date: 2024-11-06) |
| Primary citation | Afoshin, A.,Tishchenko, S.,Gabdulkhakov, A.,Kudryakova, I.,Galemina, I.,Zelenov, D.,Leontyevskaya, E.,Saharova, S.,Leontyevskaya Vasilyeva, N. Structural and Functional Characterization of beta-lytic Protease from Lysobacter capsici VKM B-2533 T. Int J Mol Sci, 23:-, 2022 Cited by PubMed Abstract: 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. PubMed: 36555752DOI: 10.3390/ijms232416100 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.57 Å) |
Structure validation
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