When adding events, the editor allows the user to specify conditions or checks that each object instance on the screen must meet before the event is added or executed. The developers also listen and take feedback from the thriving community. This work could facilitate the development of new antimicrobial compounds that disrupt WTA biosynthesis in pathogenic bacteria.Unlike many traditional development environments, Construct avoids selecting specific instances of objects when adding events to filter all instances of an object type on the screen. From these data, we present a mechanistic model of catalysis that ascribes functions for these residues. Molecular dynamics simulations and enzyme activity measurements indicate that the C-terminal polypeptide tail facilitates catalysis by encapsulating the UDP- N-acetyl- d-mannosamine substrate, presenting three highly conserved arginine residues to the active site that are important for catalysis (R214, R221, and R224). Native MS experiments support the model that only monomeric TagA is enzymatically active and that it is stabilized by membrane binding. Here, we report the crystal structure of the Thermoanaerobacter italicus TagA enzyme bound to UDP- N-acetyl- d-mannosamine, revealing the molecular basis of substrate binding. TagA contains a conserved GT26 core domain followed by a C-terminal polypeptide tail that is important for catalysis and membrane binding. The first committed step in WTA biosynthesis is catalyzed by the TagA glycosyltransferase (also called TarA), a peripheral membrane protein that produces the conserved linkage unit, which joins WTA to the cell wall peptidoglycan. Wall teichoic acid (WTA) polymers are covalently affixed to the Gram-positive bacterial cell wall and have important functions in cell elongation, cell morphology, biofilm formation, and β-lactam antibiotic resistance.
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