Structural basis for the molecular evolution of SRP-GTPase activation by protein

SRP-type GTPases deviate from other GTPases in that they are not activated by GTPase-activating proteins (GAPs). New studies show that the MinD-type protein YlxH activates the SRP-GTPase FlhF, which is involved in flagellar biosynthesis. The crystal structure of the Bacillus subtilis FlhF-effector c...

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Main Authors: Bange, Gert (Author) , Kümmerer, Nico (Author) , Grudnik, Przemyslaw (Author) , Lindner, Robert (Author) , Petzold, Georg (Author) , Kressler, Dieter (Author) , Hurt, Ed (Author) , Wild, Klemens (Author) , Sinning, Irmgard (Author)
Format: Article (Journal)
Language:English
Published: 06 November 2011
In: Nature structural & molecular biology
Year: 2011, Volume: 18, Issue: 12, Pages: 1376-1380
ISSN:1545-9985
DOI:10.1038/nsmb.2141
Online Access:Verlag, lizenzpflichtig, Volltext: https://doi.org/10.1038/nsmb.2141
Verlag, lizenzpflichtig, Volltext: https://www.nature.com/articles/nsmb.2141
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Author Notes:Gert Bange, Nico Kümmerer, Przemyslaw Grudnik, Robert Lindner, Georg Petzold, Dieter Kressler, Ed Hurt, Klemens Wild & Irmgard Sinning
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Summary:SRP-type GTPases deviate from other GTPases in that they are not activated by GTPase-activating proteins (GAPs). New studies show that the MinD-type protein YlxH activates the SRP-GTPase FlhF, which is involved in flagellar biosynthesis. The crystal structure of the Bacillus subtilis FlhF-effector complex reveals the mechanism of activation, the general concept of which may also apply to RNA-mediated activation of the SRP-GTPases Ffh and FtsY.
Item Description:Gesehen am 28.03.2022
Physical Description:Online Resource
ISSN:1545-9985
DOI:10.1038/nsmb.2141