Structural and Functional Characterization of β−lytic Protease from <i>Lysobacter capsici</i> VKM B−2533<sup>T</sup>
The crystal structure of the <i>Lysobacter capsici</i> VKM B−2533<sup>T</sup> 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 acti...
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MDPI AG
2022-12-01
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| Series: | International Journal of Molecular Sciences |
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| Online Access: | https://www.mdpi.com/1422-0067/23/24/16100 |
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| author | Alexey Afoshin Svetlana Tishchenko Azat Gabdulkhakov Irina Kudryakova Inna Galemina Dmitry Zelenov Elena Leontyevskaya Sofia Saharova Natalya Leontyevskaya (Vasilyeva) |
| author_facet | Alexey Afoshin Svetlana Tishchenko Azat Gabdulkhakov Irina Kudryakova Inna Galemina Dmitry Zelenov Elena Leontyevskaya Sofia Saharova Natalya Leontyevskaya (Vasilyeva) |
| author_sort | Alexey Afoshin |
| collection | DOAJ |
| description | The crystal structure of the <i>Lysobacter capsici</i> VKM B−2533<sup>T</sup> 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 <i>Pseudomonas aeruginosa</i>, 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. |
| first_indexed | 2024-03-09T16:19:13Z |
| format | Article |
| id | doaj.art-e0e5342994924ff8bda7f524f28d6da2 |
| institution | Directory Open Access Journal |
| issn | 1661-6596 1422-0067 |
| language | English |
| last_indexed | 2024-03-09T16:19:13Z |
| publishDate | 2022-12-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | International Journal of Molecular Sciences |
| spelling | doaj.art-e0e5342994924ff8bda7f524f28d6da22023-11-24T15:33:10ZengMDPI AGInternational Journal of Molecular Sciences1661-65961422-00672022-12-0123241610010.3390/ijms232416100Structural and Functional Characterization of β−lytic Protease from <i>Lysobacter capsici</i> VKM B−2533<sup>T</sup>Alexey Afoshin0Svetlana Tishchenko1Azat Gabdulkhakov2Irina Kudryakova3Inna Galemina4Dmitry Zelenov5Elena Leontyevskaya6Sofia Saharova7Natalya Leontyevskaya (Vasilyeva)8Laboratory 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, RussiaInstitute of Protein Research, Russian Academy of Sciences, 4 Institutskaya Str., 142290 Pushchino, RussiaInstitute of Protein Research, Russian Academy of Sciences, 4 Institutskaya Str., 142290 Pushchino, RussiaLaboratory 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, RussiaLaboratory 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, RussiaLaboratory 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, RussiaLaboratory 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, RussiaFaculty of Chemical Technology and Biotechnology, Moscow Polytechnic University, 38 Bolshaya Semyonovskaya Str., 107023 Moscow, RussiaLaboratory 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, RussiaThe crystal structure of the <i>Lysobacter capsici</i> VKM B−2533<sup>T</sup> 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 <i>Pseudomonas aeruginosa</i>, 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.https://www.mdpi.com/1422-0067/23/24/16100β−lytic protease<i>Lysobacter capsici</i>bacteriolytic enzymesBlp crystal structureLasAMRSA |
| spellingShingle | Alexey Afoshin Svetlana Tishchenko Azat Gabdulkhakov Irina Kudryakova Inna Galemina Dmitry Zelenov Elena Leontyevskaya Sofia Saharova Natalya Leontyevskaya (Vasilyeva) Structural and Functional Characterization of β−lytic Protease from <i>Lysobacter capsici</i> VKM B−2533<sup>T</sup> International Journal of Molecular Sciences β−lytic protease <i>Lysobacter capsici</i> bacteriolytic enzymes Blp crystal structure LasA MRSA |
| title | Structural and Functional Characterization of β−lytic Protease from <i>Lysobacter capsici</i> VKM B−2533<sup>T</sup> |
| title_full | Structural and Functional Characterization of β−lytic Protease from <i>Lysobacter capsici</i> VKM B−2533<sup>T</sup> |
| title_fullStr | Structural and Functional Characterization of β−lytic Protease from <i>Lysobacter capsici</i> VKM B−2533<sup>T</sup> |
| title_full_unstemmed | Structural and Functional Characterization of β−lytic Protease from <i>Lysobacter capsici</i> VKM B−2533<sup>T</sup> |
| title_short | Structural and Functional Characterization of β−lytic Protease from <i>Lysobacter capsici</i> VKM B−2533<sup>T</sup> |
| title_sort | structural and functional characterization of β lytic protease from i lysobacter capsici i vkm b 2533 sup t sup |
| topic | β−lytic protease <i>Lysobacter capsici</i> bacteriolytic enzymes Blp crystal structure LasA MRSA |
| url | https://www.mdpi.com/1422-0067/23/24/16100 |
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