Extended Data Fig. 7: Residue H305 in LnaB engages in transfer of the AMP moiety.
From: Structure and mechanism of an actin-dependent bacterial phosphoryl AMPylase
a, Two views of overall structure of the LnaB: actin: ADPR-Ub complex. The ADPR moiety is depicted in stick within orange box. b, Sectional view of a potential ADP-binding pocket formed upon PR-Ub binding. Position of the potential ADP-binding pocket is highlighted in blue circle. c, Docking models of ADP binding to the LnaB ternary complex. d, Close-up views of interactions between LnaB (cyan) and ADP. Selected hydrogen bonds are shown as blue dashed lines. e, Residue H305 of LnaB is places at a position similar to the catalytic His residue within canonical FIC proteins. Distances are shown in black dotted lines with the specific value. Residues H305 and E309 of the SHE motif from LnaB are highlighted in red. f, Evaluation of LnaB’s ATP hydrolysis capacity by different reaction time durations. Data represent mean values ± s.d. n = 3 biological replicates, p values were generated using a Student’s t- test. ns, no significant.
