title: Identification and modelling of a PPM protein phosphatase fold in the Legionella pneumophila deAMPylase SidD.
abstract: The intracellular parasitic bacterium Legionella pneumophila subverts host vesicle transport through reversible AMPylation of Rab1. The effector enzyme for deAMPylation is SidD. Here a complete PPM protein phosphatase fold catalytic domain in SidD is identified and modelled. The SidD model reveals insertions and deletions near the metal ion containing catalytic site which presumably determine its novel activity. It also sheds light on possible substrate binding residues and highlights the lack of an obvious group to act as general acid during reaction. Assignment of a PPM fold to SidD offers an important pointer towards identification of further deAMPylases.
authors.affiliation: University of Liverpool, Institute of Integrative Biology, Liverpool, UK. drigden@liv.ac.uk
authors.forename: Daniel J
authors.initials: DJ
authors.lastname: Rigden
mesh_terms: D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D016952:Legionella pneumophila / Q000201:enzymology / Q000378:metabolism*; D008969:Molecular Sequence Data; D010749:Phosphoprotein Phosphatases / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D017386:Sequence Homology, Amino Acid
chemical_list: D001426:Bacterial Proteins; C559758:SidD protein, Legionella pneumophila; D010749:Phosphoprotein Phosphatases