Extended Data Fig. 5: Conformation change of LnaB upon PR-Ub binding.
From: Structure and mechanism of an actin-dependent bacterial phosphoryl AMPylase
a, Two views of the structural superimposition of LnaB in binary complex (green) and ternary complex (pink) by αC atoms. LnaB and actin are depicted in cylindrical cartoon. PR-Ub is shown in orange ribbon. The RMSD was 0.83 Å. b, Evaluation of the role of residues involved in the activation loop in LnaB’s activity. The data represent three independent experiments. ΔAA: Alanine-substitutions in residues containing a side chain of the activation loop; Δloop: deletion of the activation loop. Residue E309 in the SHE motif is highlighted in red. c, Multiple sequence alignment of LnaB with other SHE family proteins by PROMALS3D. Listed from left to right are species, accession number, and amino acids. Identities of residues important for LnaB activity are highlighted in red. Residues composing of the activation loop are underlined. The species listed are Legionella pneumophila (L.p.), Francisella sp. W12-1067 (F.s.), Burkholderia ambifaria (B.a.), Xenorhabdus bovienii (X.b.), Photorhabdus temperate (P.t.), and Pseudomonas protegens (P.p.). d, Evaluation of the M217 mutation activities. The data represent three independent experiments.
