Publications
| Title | Abstract | Year Filter | PMID(sorted descending) Filter |
|---|
| 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- ... | 2008 | 18560152 |