8af1

Beta-Lytic Protease from Lysobacter capsiciBeta-Lytic Protease from Lysobacter capsici

Structural highlights 8af1 is a 1 chain structure with sequence from Lysobacter capsici. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.57Å Ligands: , , , Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

spinqualitylabelsall models 8af1, resolution 1.57Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image