Extended Data Figure 1: MraY catalyses the formation of lipid I and binds MD2.
From: Structural insights into inhibition of lipid I production in bacterial cell wall synthesis
a, Scheme of the reaction catalysed by MraY. The U-labelled blue hexagon represents uridine and the M-labelled orange hexagon represents MurNAc. The phosphates associated with the lipid carrier C55-P are shown as red circles, and the phosphates from the substrate, UM5A, are shown as yellow circles. b, Chemical structures of the substrate, UM5A (top) and the inhibitor MD2 (bottom). c, Michaelis–Menten kinetic characterization of MraYAA translocase activity. The reaction monitored is the MraYAA-catalysed transfer of [14C]phospho-MurNAc-pentapeptide from [14C]UM5A to C55-P, forming [14C]lipid I. The enzymatic parameters measured are as follows: Km = 190 ± 60 μM, kcat = 20 ± 2 min−1, kcat/Km = 0.11 ± 0.3 μM−1 min−1. Data are mean and s.e.m. of three technical replicates. d, MD2 (green) in complex with MraYAA. The distances between MD2 and the three catalytic acidic residues Asp117, Asp118 and Asp265 (magenta) are all greater than 4.5 Å.
