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

被引：0
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作者：
Gert Bange
Nico Kümmerer
Przemyslaw Grudnik
Robert Lindner
Georg Petzold
Dieter Kressler
Ed Hurt
Klemens Wild
Irmgard Sinning
机构：
[1] Heidelberg University Biochemistry Center,
[2] Present addresses: Research Institute of Molecular Pathology,undefined
[3] Vienna,undefined
[4] Austria (G.P.); Unit of Biochemistry,undefined
[5] University of Fribourg,undefined
[6] Fribourg,undefined
[7] Switzerland (D.K.).,undefined
来源：
Nature Structural & Molecular Biology | 2011年 / 18卷
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摘要：
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.
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页码：1376 / 1380
页数：4
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