Structural basis for the O-acetyltransferase function of the extracytoplasmic domain of OatA from Staphylococcus aureus.

ABSTRACT: Many bacteria possess enzymes that modify the essential cell-wall polymer peptidoglycan by O-acetylation. This modification occurs in numerous Gram-positive pathogens, including methicillin-resistant Staphylococcus aureus, a common cause of human infections. O-Acetylation of peptidoglycan protects bacteria from the lytic activity of lysozyme, a mammalian innate immune enzyme, and as such is important for bacterial virulence. The O-acetylating enzyme in Gram-positive bacteria, O-acetyltransferase A (OatA), is a two-domain protein consisting of an N-terminal integral membrane domain and a C-terminal extracytoplasmic domain. Here, we present the X-ray crystal structure at 1.71 Å resolution and the biochemical characterization of the C-terminal domain of S

SUBMITTER: Jones CS 

PROVIDER: S-EPMC7294091 | biostudies-literature | 2020 Jun

REPOSITORIES: biostudies-literature