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8OQ1

Crystal structure of tailspike depolymerase (APK14_gp49) from Acinetobacter phage vB_AbaP_APK14

This is a non-PDB format compatible entry.
Summary for 8OQ1
Entry DOI10.2210/pdb8oq1/pdb
DescriptorTail spike protein, structural depolymerase, DI(HYDROXYETHYL)ETHER, GLYCEROL, ... (5 entities in total)
Functional Keywordsbacteriophage, acinetobacter baumannii, tailspike depolymerase, acinetobacter phage, viral protein
Biological sourceAcinetobacter phage vB_AbaP_APK14
Total number of polymer chains1
Total formula weight79852.64
Authors
Matyuta, I.O.,Boyko, K.M.,Nikolaeva, A.Y.,Shneider, M.M.,Timoshina, O.Y.,Miroshnikov, K.A.,Popov, V.O. (deposition date: 2023-04-10, release date: 2023-06-07, Last modification date: 2024-06-19)
Primary citationTimoshina, 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: 37240444
DOI: 10.3390/ijms24109100
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.55 Å)
Structure validation

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