5MU4

Tail Tubular Protein A of Klebsiella pneumoniae bacteriophage KP32

Summary for 5MU4

• Entry DOI: 10.2210/pdb5mu4/pdb
• Descriptor: Tail tubular protein A (2 entities in total)
• Functional Keywords: tail tubular protein, bacteriophage, exopolysaccharide depolymerase, antibacterial activity, viral protein
• Biological source: Klebsiella phage KP32
• Total number of polymer chains: 4
• Total formula weight: 89126.72

Authors

Pyra, A.,Brzozowska, E.,Pawlik, K.,Dauter, M.,Dauter, Z.,Gamian, A. (deposition date: 2017-01-12, release date: 2017-05-31, Last modification date: 2024-05-08)

Primary citation

Pyra, A.,Brzozowska, E.,Pawlik, K.,Gamian, A.,Dauter, M.,Dauter, Z.
Tail tubular protein A: a dual-function tail protein of Klebsiella pneumoniae bacteriophage KP32.
Sci Rep, 7:2223-2223, 2017

PubMed Abstract: Tail tubular protein A (TTPA) is a structural tail protein of Klebsiella pneumoniae bacteriophage KP32, and is responsible for adhering the bacteriophage to host cells. For the first time, we found that TTPA also exhibits lytic activity towards capsular exopolysaccharide (EPS) of the multiresistant clinical strain of Klebsiella pneumoniae, PCM2713, and thus should be regarded as a dual-function macromolecule that exhibits both structural and enzymatic actions. Here, we present our crystallographic and enzymatic studies of TTPA. TTPA was crystallized and X-ray diffraction data were collected to a resolution of 1.9 Å. In the crystal, TTPA molecules were found to adopt a tetrameric structure with α-helical domains on one side and β-strands and loops on the other. The novel crystal structure of TTPA resembles those of the bacteriophage T7 tail protein gp11 and gp4 of bacteriophage P22, but TTPA contains an additional antiparallel β-sheet carrying a lectin-like domain that could be responsible for EPS binding. The enzymatic activity of TTPA may reflect the presence of a peptidoglycan hydrolase domain in the α-helical region (amino acid residues 126 to 173). These novel results provide new insights into the enzymatic mechanism through which TTPA acts on polysaccharides.

PubMed: 28533535
DOI: 10.1038/s41598-017-02451-3

Experimental method

X-RAY DIFFRACTION (1.9 Å)