Structure and Mechanism of LcpA, a Phosphotransferase That Mediates Glycosylation of a Gram-Positive Bacterial Cell Wall-Anchored Protein
Year: 2019
Type: article
Abstract: In Gram-positive bacteria, the conserved LCP family enzymes studied to date are known to attach glycopolymers, including wall teichoic acid, to the cell envelope. It is unknown if these enzymes catalyze glycosylation of surface proteins. We show here in the actinobacterium Actinomyces oris by X-ray crystallography and biochemical analyses that A. oris LcpA is an LCP homolog, possessing pyrophosphatase and phosphotransferase activities known to belong to LCP enzymes that require conserved catalytic Arg residues, while harboring a unique disulfide bond critical for protein stability. Importantly, LcpA mediates glycosylation of the surface protein GspA via phosphotransferase activity. Our studies provide the first experimental evidence of an archetypal LCP enzyme that promotes glycosylation of a cell wall-anchored protein in Gram-positive bacteria.
Source: mBio
Language: English
Subfield: Genetics
Domain: Life Sciences
Open Access status: gold
Estimated APC paid: $3,900
Awards: G1601226246, G2803843123, G3122633388, G3508934553, G4610968367, Molecular Assembly on the Cell Surface of Actinomyces, G6344573930, G7838705897, UCLA-DOE INSTITUTE FOR GENOMICS AND PROTEOMICS, Development of a cell-based assay to discover new bacterial anti-infective agents, Cell Surface Polymer Display in Gram-Positive Bacteria, NE-CAT: A Resource for Advanced Macromolecular Crystallography
OpenAlex ID: W2916629563