5wb4 | pdb_00005wb4

Crystal structure of the TarA wall teichoic acid glycosyltransferase

spinqualitylabelsall models 5wb4, resolution 2.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5wb4 is a 8 chain structure with sequence from Thermoanaerobacter italicus Ab9. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2Å Ligands: MSE, SO4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function D3T4E0_THEIA Catalyzes the conversion of GlcNAc-PP-undecaprenol into ManNAc-GlcNAc-PP-undecaprenol, the first committed lipid intermediate in the de novo synthesis of teichoic acid.[HAMAP-Rule:MF_02070] Publication Abstract from PubMed 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 beta-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. Structure and mechanism of TagA, a novel membrane-associated glycosyltransferase that produces wall teichoic acids in pathogenic bacteria.,Kattke MD, Gosschalk JE, Martinez OE, Kumar G, Gale RT, Cascio D, Sawaya MR, Philips M, Brown ED, Clubb RT PLoS Pathog. 2019 Apr 19;15(4):e1007723. doi: 10.1371/journal.ppat.1007723., eCollection 2019 Apr. PMID:31002736 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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