6l00

Crystal structure of the cell-wall binding domain (CBD) of endolysin LysIME-EF1

spinqualitylabelsall models 6l00, resolution 1.75Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6l00 is a 1 chain structure with sequence from Enterococcus phage IMEEF1. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.75Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function S5MRN1_9CAUD Publication Abstract from PubMed 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 A 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. Structural and functional insights into a novel two-component endolysin encoded by a single gene in Enterococcus faecalis phage.,Zhou B, Zhen X, Zhou H, Zhao F, Fan C, Perculija V, Tong Y, Mi Z, Ouyang S PLoS Pathog. 2020 Mar 16;16(3):e1008394. doi: 10.1371/journal.ppat.1008394., eCollection 2020 Mar. PMID:32176738 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Lysin 3D structures

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