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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| Auteurs principaux: | , , , , , , , , |
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| Format: | Article (Journal) |
| Langue: | anglais |
| Publié: |
06 November 2011
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| In: |
Nature structural & molecular biology
Year: 2011, Volume: 18, Numéro: 12, Pages: 1376-1380 |
| ISSN: | 1545-9985 |
| DOI: | 10.1038/nsmb.2141 |
| Accès en ligne: | Verlag, lizenzpflichtig, Volltext: https://doi.org/10.1038/nsmb.2141 Verlag, lizenzpflichtig, Volltext: https://www.nature.com/articles/nsmb.2141 
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| Notes sur l'auteur: | Gert Bange, Nico Kümmerer, Przemyslaw Grudnik, Robert Lindner, Georg Petzold, Dieter Kressler, Ed Hurt, Klemens Wild & Irmgard Sinning |
| Résumé: | 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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| Description: | Gesehen am 28.03.2022 |
| Description matérielle: | Online Resource |
| ISSN: | 1545-9985 |
| DOI: | 10.1038/nsmb.2141 |