5WB4

Crystal structure of the TarA wall teichoic acid glycosyltransferase

Summary for 5WB4

• Entry DOI: 10.2210/pdb5wb4/pdb
• Descriptor: N-acetylglucosaminyldiphosphoundecaprenol N-acetyl-beta-D-mannosaminyltransferase, SULFATE ION (3 entities in total)
• Functional Keywords: glycosyltransferase, wall teichoic acid enzyme, beta-n-acetylmannosaminyltransferase, transferase
• Biological source: Thermoanaerobacter italicus
• Total number of polymer chains: 8
• Total formula weight: 176772.16

Authors

Kattke, M.D.,Cascio, D.,Sawaya, M.R.,Clubb, R.T. (deposition date: 2017-06-27, release date: 2019-01-16, Last modification date: 2024-10-16)

Primary citation

Kattke, M.D.,Gosschalk, J.E.,Martinez, O.E.,Kumar, G.,Gale, R.T.,Cascio, D.,Sawaya, M.R.,Philips, M.,Brown, E.D.,Clubb, R.T.
Structure and mechanism of TagA, a novel membrane-associated glycosyltransferase that produces wall teichoic acids in pathogenic bacteria.
Plos Pathog., 15:e1007723-e1007723, 2019

PubMed 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 synthesize a range of extracellular polysaccharides through a poorly understood mechanism. Crystal structures of TagA from T. italicus in its apo- and UDP-bound states reveal a novel GT fold, and coupled with biochemical and cellular data define the mechanism of catalysis. We propose that enzyme activity is regulated by interactions with the bilayer, which trigger a structural change that facilitates proper active site formation and recognition of the enzyme's lipid-linked substrate. These findings inform upon the molecular basis of WecB/TagA/CpsF activity and could guide the development of new anti-microbial drugs.

PubMed: 31002736
DOI: 10.1371/journal.ppat.1007723

Experimental method

X-RAY DIFFRACTION (2 Å)