1TAD

GTPASE MECHANISM OF GPROTEINS FROM THE 1.7-ANGSTROM CRYSTAL STRUCTURE OF TRANSDUCIN ALPHA-GDP-ALF4-

1TAD の概要

• エントリーDOI: 10.2210/pdb1tad/pdb
• 分子名称: TRANSDUCIN-ALPHA, CALCIUM ION, CACODYLATE ION, ... (6 entities in total)
• 機能のキーワード: gtp-binding protein, g-protein, gtpase, transducin
• 由来する生物種: Bos taurus (cattle)
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 114005.09

構造登録者

Sondek, J.,Lambright, D.G.,Noel, J.P.,Hamm, H.E.,Sigler, P.B. (登録日: 1995-01-05, 公開日: 1995-05-08, 最終更新日: 2024-02-14)

主引用文献

Sondek, J.,Lambright, D.G.,Noel, J.P.,Hamm, H.E.,Sigler, P.B.
GTPase mechanism of Gproteins from the 1.7-A crystal structure of transducin alpha-GDP-AIF-4.
Nature, 372:276-279, 1994

PubMed Abstract: Aluminium fluoride (AIF-4) activates members of the heterotrimeric G-protein (G alpha beta gamma) family by binding to inactive G alpha.GDP near the site occupied by the gamma-phosphate in G alpha.GTP (ref. 3). Here we describe the crystal structure of transducin alpha.GDP activated with aluminium fluoride (Gt alpha.GDP.AIF-4.H2O) at 1.7 A, a resolution sufficient to establish the coordination geometry of the bound aluminium fluoride as well as the extensive network of direct and water-mediated interactions that stabilize it. These observations are derived from three independent representations in the asymmetric unit, eliminating any chance of drawing conclusions based on stereochemistry imposed by crystal packing. Surprisingly, aluminium fluoride activates G alpha.GDP by binding with a geometry resembling a pentavalent intermediate for GTP hydrolysis. The stabilizing interactions involve not only residues that interact with the gamma-phosphate in Gt alpha.GTP gamma S, but also conserved residues for GTPase activity. Thus the Gt alpha.GDP.AIF-4.H2O structure provides new insight into the mechanism of GTP hydrolysis.

PubMed: 7969474
DOI: 10.1038/372276a0

実験手法

X-RAY DIFFRACTION (1.7 Å)