Structural highlights
Publication Abstract from PubMedTail 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 A. In the crystal, TTPA molecules were found to adopt a tetrameric structure with alpha-helical domains on one side and beta-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 beta-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 alpha-helical region (amino acid residues 126 to 173). These novel results provide new insights into the enzymatic mechanism through which TTPA acts on polysaccharides. Tail tubular protein A: a dual-function tail protein of Klebsiella pneumoniae bacteriophage KP32.,Pyra A, Brzozowska E, Pawlik K, Gamian A, Dauter M, Dauter Z Sci Rep. 2017 May 22;7(1):2223. doi: 10.1038/s41598-017-02451-3. PMID:28533535[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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