5WFG

Crystal structure of the TarA wall teichoic acid glycosyltransferase bound to UDP

5WFG の概要

• エントリーDOI: 10.2210/pdb5wfg/pdb
• 分子名称: N-acetylglucosaminyldiphosphoundecaprenol N-acetyl-beta-D-mannosaminyltransferase, URIDINE-5'-DIPHOSPHATE (3 entities in total)
• 機能のキーワード: glycosyltransferase, wall teichoic acid enzyme, beta-n-acetylmannosaminyltransferase, transferase
• 由来する生物種: Thermoanaerobacter italicus
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 134548.06

構造登録者

Kattke, M.D.,Cascio, D.,Sawaya, M.R.,Clubb, R.T. (登録日: 2017-07-11, 公開日: 2019-01-16, 最終更新日: 2024-10-23)

主引用文献

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

実験手法

X-RAY DIFFRACTION (2.9 Å)