8OQ0
Crystal structure of tailspike depolymerase (APK09_gp48) from Acinetobacter phage APK09
Summary for 8OQ0
| Entry DOI | 10.2210/pdb8oq0/pdb |
| Descriptor | Tailspike protein, DI(HYDROXYETHYL)ETHER (3 entities in total) |
| Functional Keywords | bacteriophage, acinetobacter baumannii, tailspike depolymerase, viral protein |
| Biological source | Acinetobacter phage APK09 |
| Total number of polymer chains | 1 |
| Total formula weight | 66704.44 |
| Authors | Matyuta, I.O.,Boyko, K.M.,Nikolaeva, A.Y.,Shneider, M.M.,Timoshina, O.Y.,Popova, A.V.,Miroshnikov, K.A.,Popov, V.O. (deposition date: 2023-04-10, release date: 2023-05-31, Last modification date: 2024-06-19) |
| Primary citation | Timoshina, O.Y.,Kasimova, A.A.,Shneider, M.M.,Matyuta, I.O.,Nikolaeva, A.Y.,Evseev, P.V.,Arbatsky, N.P.,Shashkov, A.S.,Chizhov, A.O.,Shelenkov, A.A.,Mikhaylova, Y.V.,Slukin, P.V.,Volozhantsev, N.V.,Boyko, K.M.,Knirel, Y.A.,Miroshnikov, K.A.,Popova, A.V. Friunavirus Phage-Encoded Depolymerases Specific to Different Capsular Types of Acinetobacter baumannii . Int J Mol Sci, 24:-, 2023 Cited by PubMed Abstract: is a critical priority nosocomial pathogen that produces a variety of capsular polysaccharides (CPSs), the primary receptors for specific depolymerase-carrying phages. In this study, the tailspike depolymerases (TSDs) encoded in genomes of six novel Friunaviruses, APK09, APK14, APK16, APK86, APK127v, APK128, and one previously described phage, APK37.1, were characterized. For all TSDs, the mechanism of specific cleavage of corresponding capsular polysaccharides (CPSs) was established. The structures of oligosaccharide fragments derived from K9, K14, K16, K37/K3-v1, K86, K127, and K128 CPSs degradation by the recombinant depolymerases have been determined. The crystal structures of three of the studied TSDs were obtained. A significant reduction in mortality of larvae infected with of K9 capsular type was shown in the example of recombinant TSD APK09_gp48. The data obtained will provide a better understanding of the interaction of phage-bacterial host systems and will contribute to the formation of principles of rational usage of lytic phages and phage-derived enzymes as antibacterial agents. PubMed: 37240444DOI: 10.3390/ijms24109100 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.59 Å) |
Structure validation
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