1GWN

The crystal structure of the core domain of RhoE/Rnd3 - a constitutively activated small G protein

1GWN の概要

• エントリーDOI: 10.2210/pdb1gwn/pdb
• 分子名称: Rho-related GTP-binding protein RhoE, GUANOSINE-5'-TRIPHOSPHATE, MAGNESIUM ION, ... (4 entities in total)
• 機能のキーワード: gtpase, inactive gtpase, signal transduction
• 由来する生物種: Mus musculus (Mouse)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 46820.46

構造登録者

Garavini, H.,Riento, K.,Phelan, J.P.,McAlister, M.S.B.,Ridley, A.J.,Keep, N.H. (登録日: 2002-03-19, 公開日: 2002-04-05, 最終更新日: 2024-11-13)

主引用文献

Garavini, H.,Riento, K.,Phelan, J.P.,McAlister, M.S.B.,Ridley, A.J.,Keep, N.H.
Crystal Structure of the Core Domain of Rhoe/Rnd3: A Constitutively Activated Small G Protein
Biochemistry, 41:6303-6310, 2002

PubMed Abstract: We report the 2.1 A crystal structure of the core G protein domain of the unusual Rho family member RhoE/Rnd3 in complex with endogenous GTP and magnesium. Unlike other small G proteins, RhoE, along with two other proteins Rnd1/Rho6 and Rnd2/RhoN, does not hydrolyze GTP. The main reason for this is the presence of serines in the positions equivalent to Ala59 and Gln61 in Ras. The structure shows that there are still water molecules in similar positions to the waters thought to be involved in the hydrolysis reaction in other G proteins. The structure suggests three not necessarily exclusive explanations for the lack of hydrolysis. The lack of the conserved glutamine raises the energy of the transition state inhibiting hydrolysis. The serines may restrain the waters from moving closer to the GTP, a step that is required to attain the transition state. They also stabilize the GTP-bound conformation of switch II and could prevent conformational changes required during hydrolysis. By superposition of the RhoE structure on structures of Rho family proteins in complex with binding partners, we make predictions on RhoE interactions with these partners.

PubMed: 12009891
DOI: 10.1021/BI025651H

実験手法

X-RAY DIFFRACTION (2.1 Å)