7D55
Crystal structure of lys170 CBD
Summary for 7D55
| Entry DOI | 10.2210/pdb7d55/pdb |
| Descriptor | Putative N-acetylmuramoyl-L-alanine amidase (2 entities in total) |
| Functional Keywords | lysin, hydrolase |
| Biological source | Enterococcus phage phiM1EF22 |
| Total number of polymer chains | 4 |
| Total formula weight | 41563.58 |
| Authors | Zhen, X. (deposition date: 2020-09-25, release date: 2021-06-09, Last modification date: 2024-03-27) |
| Primary citation | Xu, X.,Zhang, D.,Zhou, B.,Zhen, X.,Ouyang, S. Structural and biochemical analyses of the tetrameric cell binding domain of Lys170 from enterococcal phage F170/08. Eur.Biophys.J., 50:721-729, 2021 Cited by PubMed Abstract: Lysins are a class of hydrolytic enzymes used by bacteriophages to target and cleave the peptidoglycan of bacterial cell walls during their lytic cycle. The lysins from bacteriophages that infect Gram-positive bacteria are typically monomeric and consist of one or two catalytic domains (CD) and a cell binding domain (CBD). However, multimeric lysins encoded by a single gene have also been reported, among which Lys170 from enterococcal phage F170/08 was one of the first identified. Here, we determined the crystal structure of Lys170 CBD at 1.40 Å resolution. The structure reveals that Lys170 CBDs assemble into a tetrameric functional unit and that each monomer folds into a three-stranded β-sheet core capped on each side by an α-helix. In addition, we identified key residues of Lys170 CBD involved in host cell binding. Our work provides a basis for designing highly efficient lysins targeting Enterococcus faecalis. PubMed: 33609147DOI: 10.1007/s00249-021-01511-x PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.397 Å) |
Structure validation
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