8K6F
LnaB-Actin-PRUb ternary complex
8K6F の概要
| エントリーDOI | 10.2210/pdb8k6f/pdb |
| 分子名称 | Actin gamma 1, Legionella effector LnaB, Ubiquitin, ... (5 entities in total) |
| 機能のキーワード | ampylation, legionella effector, toxin |
| 由来する生物種 | Legionella 詳細 |
| タンパク質・核酸の鎖数 | 6 |
| 化学式量合計 | 183650.83 |
| 構造登録者 | |
| 主引用文献 | Chen, T.T.,Lu, Q.,Zheng, S.R.,Fu, J.,Chen, J.,Kang, L.,Wu, J.,Luo, J.,Tong, J.,Li, S.,Li, X.,Li, S.,Li, J.,Wang, S.,Feng, Y.,Luo, Z.Q.,Ouyang, S. Structure and mechanism of an actin-dependent bacterial phosphoryl AMPylase. Nat.Chem.Biol., 2025 Cited by PubMed Abstract: The two effectors LnaB and MavL of Legionella pneumophila coordinate the conversion of phosphoribosyl ubiquitin (PR-Ub) released by reversal of ubiquitination induced by members of the SidE effector family into functional Ub. LnaB acts as an actin-dependent phosphoryl AMPylase that converts PR-Ub into ADP-ribosylated (ADPR)-Ub. Catalysis by LnaB requires the conserved SHE motif present in a large family of bacterial toxins. Here we describe a series of structures of LnaB in complex with the cofactor actin and the substrate PR-Ub and ATP. LnaB harbors both adenylyltransferase and ATPase activities, which reveal an adenylylation mechanism involved in a two-step catalytic process. Actin performs a unique activation mechanism that promotes the recruitment of PR-Ub by LnaB to activate LnaB's ATPase activity through interacting with LnaB and PR-Ub. Mechanisms derived from this series of structures covering the process of LnaB action establish an important biochemical basis for protein AMPylation. PubMed: 40588486DOI: 10.1038/s41589-025-01945-w 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (3.41 Å) |
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