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TitleLegionella effector LnaB is a phosphoryl AMPylase that impairs phosphosignalling.
Journal, issue, pagesNature, Vol. 631, Issue 8020, Page 393-401, Year 2024
Publish dateMay 22, 2024
AuthorsTing Wang / Xiaonan Song / Jiaxing Tan / Wei Xian / Xingtong Zhou / Mingru Yu / Xiaofei Wang / Yan Xu / Ting Wu / Keke Yuan / Yu Ran / Bing Yang / Gaofeng Fan / Xiaoyun Liu / Yan Zhou / Yongqun Zhu /
PubMed AbstractAMPylation is a post-translational modification in which AMP is added to the amino acid side chains of proteins. Here we show that, with ATP as the ligand and actin as the host activator, the ...AMPylation is a post-translational modification in which AMP is added to the amino acid side chains of proteins. Here we show that, with ATP as the ligand and actin as the host activator, the effector protein LnaB of Legionella pneumophila exhibits AMPylase activity towards the phosphoryl group of phosphoribose on PR-Ub that is generated by the SidE family of effectors, and deubiquitinases DupA and DupB in an E1- and E2-independent ubiquitination process. The product of LnaB is further hydrolysed by an ADP-ribosylhydrolase, MavL, to Ub, thereby preventing the accumulation of PR-Ub and ADPR-Ub and protecting canonical ubiquitination in host cells. LnaB represents a large family of AMPylases that adopt a common structural fold, distinct from those of the previously known AMPylases, and LnaB homologues are found in more than 20 species of bacterial pathogens. Moreover, LnaB also exhibits robust phosphoryl AMPylase activity towards phosphorylated residues and produces unique ADPylation modifications in proteins. During infection, LnaB AMPylates the conserved phosphorylated tyrosine residues in the activation loop of the Src family of kinases, which dampens downstream phosphorylation signalling in the host. Structural studies reveal the actin-dependent activation and catalytic mechanisms of the LnaB family of AMPylases. This study identifies, to our knowledge, an unprecedented molecular regulation mechanism in bacterial pathogenesis and protein phosphorylation.
External linksNature / PubMed:38776962
MethodsEM (single particle) / X-ray diffraction
Resolution2.66 - 3.04 Å
Structure data

36454

8jo3

EMDB-36454, PDB-8jo3:
Cryo-EM structure of a Legionella effector complexed with actin and AMP
Method: EM (single particle) / Resolution: 2.66 Å

36455

8jo4

EMDB-36455, PDB-8jo4:
Cryo-EM structure of a Legionella effector complexed with actin and ATP
Method: EM (single particle) / Resolution: 3.04 Å

PDB-8xep:
Crystal structure of a Legionella pneumophila type IV effector in complex with ubiquitin
Method: X-RAY DIFFRACTION / Resolution: 2.95 Å

Chemicals

ChemComp-AMP:
ADENOSINE MONOPHOSPHATE / AMP*YM

ChemComp-CA:
Unknown entry

ChemComp-ATP:
ADENOSINE-5'-TRIPHOSPHATE / ATP, energy-carrying molecule*YM

ChemComp-MG:
Unknown entry

ChemComp-SO4:
SULFATE ION

Source
  • legionella sainthelensi (bacteria)
  • oryctolagus cuniculus (rabbit)
  • legionella pneumophila subsp. pneumophila str. philadelphia 1 (bacteria)
  • homo sapiens (human)
KeywordsTOXIN / AMPylation / HYDROLASE / Legionella pneumophila / type IV effector / ubiquitin / ARHs

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