| First Author | Bange G | Year | 2011 |
| Journal | Nat Struct Mol Biol | Volume | 18 |
| Issue | 12 | Pages | 1376-80 |
| PubMed ID | 22056770 | Mgi Jnum | J:247427 |
| Mgi Id | MGI:5926913 | Doi | 10.1038/nsmb.2141 |
| Citation | Bange G, et al. (2011) Structural basis for the molecular evolution of SRP-GTPase activation by protein. Nat Struct Mol Biol 18(12):1376-80 |
| abstractText | Small G proteins have key roles in signal transduction pathways. They are switched from the signaling 'on' to the non-signaling 'off' state when GTPase-activating proteins (GAPs) provide a catalytic residue. The ancient signal recognition particle (SRP)-type GTPases form GTP-dependent homo- and heterodimers and deviate from the canonical switch paradigm in that no GAPs have been identified. Here we show that the YlxH protein activates the SRP-GTPase FlhF. The crystal structure of the Bacillus subtilis FlhF-effector complex revealed that the effector does not contribute a catalytic residue but positions the catalytic machinery already present in SRP-GTPases. We provide a general concept that might also apply to the RNA-driven activation of the universally conserved, co-translational protein-targeting machinery comprising the SRP-GTPases Ffh and FtsY. Our study exemplifies the evolutionary transition from RNA- to protein-driven activation in SRP-GTPases and suggests that the current view on SRP-mediated protein targeting is incomplete. |
