8K6V
LnaB-Actin-PRUb ternary complex
Summary for 8K6V
| Entry DOI | 10.2210/pdb8k6v/pdb |
| Descriptor | Actin gamma 1, LnaB, Ubiquitin, ... (6 entities in total) |
| Functional Keywords | ampylation, legionella effector, toxin |
| Biological source | Legionella More |
| Total number of polymer chains | 3 |
| Total formula weight | 92104.09 |
| Authors | Chen, T.T.,Ouyang, S.Y. (deposition date: 2023-07-25, release date: 2025-01-29, Last modification date: 2025-08-13) |
| Primary citation | 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 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.6 Å) |
Structure validation
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