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• W2016228685 abstract "The causative agent of Legionnaires disease, Legionella pneumophila , injects several hundred proteins into the cell it infects, many of which interfere with or exploit vesicular transport processes. One of these proteins, LidA, has been described as a Rab effector (i.e., a molecule that interacts preferentially with the GTP-bound form of Rab). We describe here the structure and biochemistry of a complex between the Rab-binding domain of LidA and active Rab8a. LidA displays structural peculiarities in binding to Rab8a, forming a considerably extended interface in comparison to known mammalian Rab effectors, and involving regions of the GTPase that are not seen in other Rab:effector complexes. In keeping with this extended binding interface, which involves four α-helices and two pillar-like structures of LidA, the stability of LidA-Rab interactions is dramatically greater than for other such complexes. For Rab1b and Rab8a, these affinities are extraordinarily high, but for the more weakly bound Rab6a, K d values of 4 nM for the inactive and 30 pM for the active form were found. Rab1b and Rab8a appear to bind LidA with K d values in the low picomolar range, making LidA a Rab supereffector." @default.
• W2016228685 created "2016-06-24" @default.
• W2016228685 creator A5046667100 @default.
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• W2016228685 creator A5068541764 @default.
• W2016228685 creator A5091424308 @default.
• W2016228685 date "2011-10-19" @default.
• W2016228685 modified "2023-10-16" @default.
• W2016228685 title "Protein LidA from Legionella is a Rab GTPase supereffector" @default.
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• W2016228685 doi "https://doi.org/10.1073/pnas.1113133108" @default.
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