8ipw | pdb_00008ipw

The sturecture of Legionella effector protein MavL with ADPR

spinqualitylabelsall models 8ipw, resolution 2.35Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 8ipw is a 2 chain structure with sequence from Legionella pneumophila. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.35Å Ligands: AR6 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q5ZSJ1_LEGPH Publication Abstract from PubMed 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. Legionella maintains host cell ubiquitin homeostasis by effectors with unique catalytic mechanisms.,Fu J, Li S, Guan H, Li C, Zhao YB, Chen TT, Xian W, Zhang Z, Liu Y, Guan Q, Wang J, Lu Q, Kang L, Zheng SR, Li J, Cao S, Das C, Liu X, Song L, Ouyang S, Luo ZQ Nat Commun. 2024 Jul 15;15(1):5953. doi: 10.1038/s41467-024-50311-2. PMID:39009586 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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