8IPJ
Crystal structure of the Legionella effector protein MavL with ADPR-Ub
8IPJ の概要
| エントリーDOI | 10.2210/pdb8ipj/pdb |
| 分子名称 | MavL, Ubiquitin, [(2R,3S,4R,5R)-5-(6-AMINOPURIN-9-YL)-3,4-DIHYDROXY-OXOLAN-2-YL]METHYL[HYDROXY-[[(2R,3S,4R,5S)-3,4,5-TRIHYDROXYOXOLAN-2-YL]METHOXY]PHOSPHORYL] HYDROGEN PHOSPHATE, ... (4 entities in total) |
| 機能のキーワード | mavl, adpr-ub, protein binding |
| 由来する生物種 | Legionella pneumophila 詳細 |
| タンパク質・核酸の鎖数 | 2 |
| 化学式量合計 | 49377.43 |
| 構造登録者 | |
| 主引用文献 | Fu, J.,Li, S.,Guan, H.,Li, C.,Zhao, Y.B.,Chen, T.T.,Xian, W.,Zhang, Z.,Liu, Y.,Guan, Q.,Wang, J.,Lu, Q.,Kang, L.,Zheng, S.R.,Li, J.,Cao, S.,Das, C.,Liu, X.,Song, L.,Ouyang, S.,Luo, Z.Q. Legionella maintains host cell ubiquitin homeostasis by effectors with unique catalytic mechanisms. Nat Commun, 15:5953-5953, 2024 Cited by PubMed Abstract: The intracellular bacterial pathogen Legionella pneumophila modulates host cell functions by secreting multiple effectors with diverse biochemical activities. In particular, effectors of the SidE family interfere with host protein ubiquitination in a process that involves production of phosphoribosyl ubiquitin (PR-Ub). Here, we show that effector LnaB converts PR-Ub into ADP-ribosylated ubiquitin, which is further processed to ADP-ribose and functional ubiquitin by the (ADP-ribosyl)hydrolase MavL, thus maintaining ubiquitin homeostasis in infected cells. Upon being activated by actin, LnaB also undergoes self-AMPylation on tyrosine residues. The activity of LnaB requires a motif consisting of Ser, His and Glu (SHxxxE) present in a large family of toxins from diverse bacterial pathogens. Thus, our study sheds light on the mechanisms by which a pathogen maintains ubiquitin homeostasis and identifies a family of enzymes capable of protein AMPylation. PubMed: 39009586DOI: 10.1038/s41467-024-50311-2 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.003 Å) |
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