2RGC

Crystal structure of H-RasQ61V-GppNHp

2RGC の概要

• エントリーDOI: 10.2210/pdb2rgc/pdb
• 関連するPDBエントリー: 2RGA 2RGB 2RGD 2RGE 2RGG
• 分子名称: GTPase HRas, MAGNESIUM ION, CALCIUM ION, ... (5 entities in total)
• 機能のキーワード: molecular switch protein, oncogene, signaling protein, gtpase, disease mutation, golgi apparatus, gtp-binding, lipoprotein, membrane, methylation, nucleotide-binding, palmitate, prenylation, proto-oncogene, oncoprotein
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Cell membrane; Lipid-anchor; Cytoplasmic side: P01112
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 19457.08

構造登録者

Buhrman, G.,Wink, G.,Mattos, C. (登録日: 2007-10-03, 公開日: 2007-12-18, 最終更新日: 2023-08-30)

主引用文献

Buhrman, G.,Wink, G.,Mattos, C.
Transformation Efficiency of RasQ61 Mutants Linked to Structural Features of the Switch Regions in the Presence of Raf.
Structure, 15:1618-1629, 2007

PubMed Abstract: Transformation efficiencies of Ras mutants at residue 61 range over three orders of magnitude, but the in vitro GTPase activity decreases 10-fold for all mutants. We show that Raf impairs the GTPase activity of RasQ61L, suggesting that the Ras/Raf complex differentially modulates transformation. Our crystal structures show that, in transforming mutants, switch II takes part in a network of hydrophobic interactions burying the nucleotide and precatalytic water molecule. Our results suggest that Y32 and a water molecule bridging it to the gamma-phosphate in the wild-type structure play a role in GTP hydrolysis in lieu of the Arg finger in the absence of GAP. The bridging water molecule is absent in the transforming mutants, contributing to the burying of the nucleotide. We propose a mechanism for intrinsic hydrolysis in Raf-bound Ras and elucidate structural features in the Q61 mutants that correlate with their potency to transform cells.

PubMed: 18073111
DOI: 10.1016/j.str.2007.10.011

実験手法

X-RAY DIFFRACTION (1.6 Å)