structural analysis of the l-alanoyl-d-glutamate endopeptidase domain of listeria bacteriophage endolysin ply500 reveals a new member of the las peptidase family.similar to many other bacterial cell-wall-hydrolyzing enzymes, the listeria bacteriophage a500 endopeptidase ply500 has a modular architecture consisting of an enzymatically active domain (ead) linked to a cell-wall-binding domain (cbd) in a single polypeptide chain. the crystal structure of the ead of ply500 has been solved at 1.8 a resolution. the shape of the enzyme resembles a sofa chair: one alpha-helix and three antiparallel beta-strands form the seat, which is supported by two more alpha- ...200818560152
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