| 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 |
| bacteriophage receptors on listeria monocytogenes cells are the n-acetylglucosamine and rhamnose substituents of teichoic acids or the peptidoglycan itself. | different approaches were used to examine the function of teichoic acids (ta) as phage receptors among selected listeria strains, and to identify and characterize specific receptor structures of host cells belonging to different serovars. this included successive removal of cell wall constituents, preparation and purification of ta, and glc analysis of ta components. adsorption of listeria monocytogenes bacteriophages could be inhibited by polyvalent antisera, specific lectins and addition of pu ... | 1996 | 8936325 |