3SYN

Crystal structure of FlhF in complex with its activator

Summary for 3SYN

• Entry DOI: 10.2210/pdb3syn/pdb
• Related: 2PX0 2PX3
• Descriptor: Flagellar biosynthesis protein flhF, ATP-binding protein YlxH, GUANOSINE-5'-DIPHOSPHATE, ... (7 entities in total)
• Functional Keywords: srp gtpase, flagellum, protein transport, biosynthetic protein, gtpase activating protein, type 3 secretion system, gtp-binding protein
• Biological source: Bacillus subtilis; More
• Cellular location: Cell membrane; Peripheral membrane protein; Cytoplasmic side (By similarity): Q01960
• Total number of polymer chains: 8
• Total formula weight: 148757.08

Authors

Bange, G.,Kuemmerer, N.,Wild, K.,Sinning, I. (deposition date: 2011-07-18, release date: 2011-11-09, Last modification date: 2023-09-13)

Primary citation

Bange, G.,Kummerer, N.,Grudnik, P.,Lindner, R.,Petzold, G.,Kressler, D.,Hurt, E.,Wild, K.,Sinning, I.
Structural basis for the molecular evolution of SRP-GTPase activation by protein.
Nat.Struct.Mol.Biol., 18:1376-1380, 2011

PubMed Abstract: 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.

PubMed: 22056770
DOI: 10.1038/nsmb.2141

Experimental method

X-RAY DIFFRACTION (3.063 Å)