6IST
Crystal structure of a wild type endolysin LysIME-EF1
Summary for 6IST
| Entry DOI | 10.2210/pdb6ist/pdb |
| Descriptor | Lysin, CALCIUM ION, ... (4 entities in total) |
| Functional Keywords | lysin, hydrolase |
| Biological source | Enterococcus phage IMEEF1 More |
| Total number of polymer chains | 4 |
| Total formula weight | 50815.98 |
| Authors | Ouyang, S.Y. (deposition date: 2018-11-19, release date: 2019-11-20, Last modification date: 2024-03-27) |
| Primary citation | Zhou, B.,Zhen, X.,Zhou, H.,Zhao, F.,Fan, C.,Perculija, V.,Tong, Y.,Mi, Z.,Ouyang, S. Structural and functional insights into a novel two-component endolysin encoded by a single gene in Enterococcus faecalis phage. Plos Pathog., 16:e1008394-e1008394, 2020 Cited by PubMed Abstract: Using bacteriophage-derived endolysins as an alternative strategy for fighting drug-resistant bacteria has recently been garnering renewed interest. However, their application is still hindered by their narrow spectra of activity. In our previous work, we demonstrated that the endolysin LysIME-EF1 possesses efficient bactericidal activity against multiple strains of Enterococcus faecalis (E. faecalis). Herein, we observed an 8 kDa fragment and hypothesized that it contributes to LysIME-EF1 lytic activity. To examine our hypothesis, we determined the structure of LysIME-EF1 at 1.75 Å resolution. LysIME-EF1 exhibits a unique architecture in which one full-length LysIME-EF1 forms a tetramer with three additional C-terminal cell-wall binding domains (CBDs) that correspond to the abovementioned 8 kDa fragment. Furthermore, we identified an internal ribosomal binding site (RBS) and alternative start codon within LysIME-EF1 gene, which are demonstrated to be responsible for the translation of the truncated CBD. To elucidate the molecular mechanism for the lytic activity of LysIME-EF1, we combined mutagenesis, lytic activity assays and in vivo animal infection experiments. The results confirmed that the additional LysIME-EF1 CBDs are important for LysIME-EF1 architecture and its lytic activity. To our knowledge, this is the first determined structure of multimeric endolysin encoded by a single gene in E. faecalis phages. As such, it may provide valuable insights into designing potent endolysins against the opportunistic pathogen E. faecalis. PubMed: 32176738DOI: 10.1371/journal.ppat.1008394 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.75 Å) |
Structure validation
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