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Low et al, The Journal of Biological Chemistry.

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Presentation on theme: "Low et al, The Journal of Biological Chemistry."— Presentation transcript:

1 Structure and Lytic Activity of a Bacillus anthracis Prophage Endolysin
Low et al, The Journal of Biological Chemistry. Protein: N-acetylmuramoyl-L-alanine amidase (PlyL), λ Ba02 endolysin Uniprot: Q81WA9 Evidence Code: IDA GO: , peptidoglycan catabolic process (biological process) GO: , N-acetylmuramoyl-L-alanine amidase activity (molecular function) Transfers: Hakuna, Megatron, Eyuki Petidoglycan subjected to PlyL; graph shows release of Alanine due to PlyL cleaving the amide bond between N-acetylmuramic acid and L-alanine

2 Comparison of crystal structure of PlyL with other endolysins.
Bacillus Prophage Endolysin Structure Time course assay where (PlyL) lysed 4 different bacillus species cultures within 400 seconds. Figure A, full-length. Figure B, N-Terminal.


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