Ontology highlight
ABSTRACT:
SUBMITTER: Perez-Dorado I
PROVIDER: S-EPMC6902435 | biostudies-literature | 2010 May
REPOSITORIES: biostudies-literature
Nature structural & molecular biology 20100418 5
The first structure of a pneumococcal autolysin, that of the LytC lysozyme, has been solved in ternary complex with choline and a pneumococcal peptidoglycan (PG) fragment. The active site of the hydrolase module is not fully exposed but is oriented toward the choline-binding module, which accounts for its unique in vivo features in PG hydrolysis, its activation and its regulatory mechanisms. Because of the unusual hook-shaped conformation of the multimodular protein, it is only able to hydrolyze ...[more]