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Structure and mechanism of TagA, a novel...
Journal article

Structure and mechanism of TagA, a novel membrane-associated glycosyltransferase that produces wall teichoic acids in pathogenic bacteria

Abstract

Staphylococcus aureus and other bacterial pathogens affix wall teichoic acids (WTAs) to their surface. These highly abundant anionic glycopolymers have critical functions in bacterial physiology and their susceptibility to β-lactam antibiotics. The membrane-associated TagA glycosyltransferase (GT) catalyzes the first-committed step in WTA biosynthesis and is a founding member of the WecB/TagA/CpsF GT family, more than 6,000 enzymes that …

Authors

Kattke MD; Gosschalk JE; Martinez OE; Kumar G; Gale RT; Cascio D; Sawaya MR; Philips M; Brown ED; Clubb RT

Journal

PLOS Pathogens, Vol. 15, No. 4,

Publisher

Public Library of Science (PLoS)

DOI

10.1371/journal.ppat.1007723

ISSN

1553-7366