University of Liverpool, Institute of Integrative Biology, Liverpool, UK.
FEBS Lett. 2011 Sep 2;585(17):2749-54. doi: 10.1016/j.febslet.2011.08.006. Epub 2011 Aug 11.
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.
细胞内寄生细菌军团菌通过 Rab1 的可逆 AMP 化来颠覆宿主囊泡运输。脱 AMP 化的效应酶是 SidD。在这里，鉴定并构建了 SidD 中完整的 PPM 蛋白磷酸酶折叠催化结构域。SidD 模型揭示了靠近含有金属离子的催化位点的插入和缺失，这可能决定了其新颖的活性。它还阐明了可能的底物结合残基，并突出了在反应过程中缺乏明显的基团作为通用酸。将 PPM 折叠分配给 SidD 为进一步鉴定脱 AMP 酶提供了重要线索。
