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Identification and modelling of a PPM protein phosphatase fold in theLegionella pneumophiladeAMPylase SidD

Authors
Journal
FEBS Letters
0014-5793
Publisher
Wiley Blackwell (John Wiley & Sons)
Publication Date
Volume
585
Issue
17
Identifiers
DOI: 10.1016/j.febslet.2011.08.006
Keywords
  • Ampylation
  • Adenylylation
  • Ppm Protein Phosphatase
  • Distant Homology
  • Post-Translational Modification
  • Orfan
Disciplines
  • Biology

Abstract

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.

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