1K5D

Crystal structure of Ran-GPPNHP-RanBP1-RanGAP complex

1K5D の概要

• エントリーDOI: 10.2210/pdb1k5d/pdb
• 関連するPDBエントリー: 1K5G
• 分子名称: GTP-binding nuclear protein RAN, Ran-specific GTPase-activating protein, Ran GTPase activating protein 1, ... (6 entities in total)
• 機能のキーワード: ran, ranbp1, rangap, gap, signal transduction, nuclear transport, gtp hydrolysis, ground state, complex (gtp-binding-gtpase activation), signaling protein-signaling activator complex, signaling protein/signaling activator
• 由来する生物種: Homo sapiens (human); 詳細
• 細胞内の位置: Nucleus: P62826; Cytoplasm: P41391
• タンパク質・核酸の鎖数: 12
• 化学式量合計: 366509.83

構造登録者

Seewald, M.J.,Koerner, C.,Wittinghofer, A.,Vetter, I.R. (登録日: 2001-10-10, 公開日: 2002-02-13, 最終更新日: 2023-08-16)

主引用文献

Seewald, M.J.,Korner, C.,Wittinghofer, A.,Vetter, I.R.
RanGAP mediates GTP hydrolysis without an arginine finger.
Nature, 415:662-666, 2002

PubMed Abstract: GTPase-activating proteins (GAPs) increase the rate of GTP hydrolysis on guanine nucleotide-binding proteins by many orders of magnitude. Studies with Ras and Rho have elucidated the mechanism of GAP action by showing that their catalytic machinery is both stabilized by GAP binding and complemented by the insertion of a so-called 'arginine finger' into the phosphate-binding pocket. This has been proposed as a universal mechanism for GAP-mediated GTP hydrolysis. Ran is a nuclear Ras-related protein that regulates both transport between the nucleus and cytoplasm during interphase, and formation of the mitotic spindle and/or nuclear envelope in dividing cells. Ran-GTP is hydrolysed by the combined action of Ran-binding proteins (RanBPs) and RanGAP. Here we present the three-dimensional structure of a Ran-RanBP1-RanGAP ternary complex in the ground state and in a transition-state mimic. The structure and biochemical experiments show that RanGAP does not act through an arginine finger, that the basic machinery for fast GTP hydrolysis is provided exclusively by Ran and that correct positioning of the catalytic glutamine is essential for catalysis.

PubMed: 11832950
DOI: 10.1038/415662a

実験手法

X-RAY DIFFRACTION (2.7 Å)