3SYN
Crystal structure of FlhF in complex with its activator
3SYN の概要
エントリーDOI | 10.2210/pdb3syn/pdb |
関連するPDBエントリー | 2PX0 2PX3 |
分子名称 | Flagellar biosynthesis protein flhF, ATP-binding protein YlxH, GUANOSINE-5'-DIPHOSPHATE, ... (7 entities in total) |
機能のキーワード | srp gtpase, flagellum, protein transport, biosynthetic protein, gtpase activating protein, type 3 secretion system, gtp-binding protein |
由来する生物種 | Bacillus subtilis 詳細 |
細胞内の位置 | Cell membrane; Peripheral membrane protein; Cytoplasmic side (By similarity): Q01960 |
タンパク質・核酸の鎖数 | 8 |
化学式量合計 | 148757.08 |
構造登録者 | |
主引用文献 | 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 Cited by 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: 22056770DOI: 10.1038/nsmb.2141 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (3.063 Å) |
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