8BKE
Crystal structure of the Klebsiella phage KP34p57 capsular depolymerase
This is a non-PDB format compatible entry.
Summary for 8BKE
| Entry DOI | 10.2210/pdb8bke/pdb |
| Descriptor | Uncharacterized protein 57 (2 entities in total) |
| Functional Keywords | phage, capsulae, viral protein |
| Biological source | Klebsiella phage KP34 |
| Total number of polymer chains | 2 |
| Total formula weight | 135413.28 |
| Authors | Berisio, R.,Squeglia, F. (deposition date: 2022-11-09, release date: 2023-08-30, Last modification date: 2024-03-20) |
| Primary citation | Maciejewska, B.,Squeglia, F.,Latka, A.,Privitera, M.,Olejniczak, S.,Switala, P.,Ruggiero, A.,Marasco, D.,Kramarska, E.,Drulis-Kawa, Z.,Berisio, R. Klebsiella phage KP34gp57 capsular depolymerase structure and function: from a serendipitous finding to the design of active mini-enzymes against K. pneumoniae. Mbio, 14:e0132923-e0132923, 2023 Cited by PubMed Abstract: In this work, we determined the structure of phage KP34p57 capsular depolymerase and dissected the role of individual domains in trimerization and functional activity. The crystal structure serendipitously revealed that the enzyme can exist in a monomeric state once deprived of its C-terminal domain. Based on the crystal structure and site-directed mutagenesis, we localized the key catalytic residues in an intra-subunit deep groove. Consistently, we show that C-terminally trimmed KP34p57 variants are monomeric, stable, and fully active. The elaboration of monomeric, fully active phage depolymerases is innovative in the field, as no previous example exists. Indeed, mini phage depolymerases can be combined in chimeric enzymes to extend their activity ranges, allowing their use against multiple serotypes. PubMed: 37707438DOI: 10.1128/mbio.01329-23 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
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