1GDD

TERTIARY AND QUATERNARY STRUCTURAL CHANGES IN GIA1 INDUCED BY GTP HYDROLYSIS

1GDD の概要

• エントリーDOI: 10.2210/pdb1gdd/pdb
• 分子名称: GI ALPHA 1, SULFATE ION, GUANOSINE-5'-DIPHOSPHATE, ... (4 entities in total)
• 機能のキーワード: gtp-ase, signal transduction protein
• 由来する生物種: Rattus norvegicus (Norway rat)
• 細胞内の位置: Nucleus: P10824
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 40807.10

構造登録者

Mixon, M.B.,Sprang, S.R. (登録日: 1995-07-25, 公開日: 1995-11-27, 最終更新日: 2024-02-07)

主引用文献

Mixon, M.B.,Lee, E.,Coleman, D.E.,Berghuis, A.M.,Gilman, A.G.,Sprang, S.R.
Tertiary and quaternary structural changes in Gi alpha 1 induced by GTP hydrolysis.
Science, 270:954-960, 1995

PubMed Abstract: Crystallographic analysis of 2.2 angstrom resolution shows that guanosine triphosphate (GTP) hydrolysis triggers conformational changes in the heterotrimeric G-protein alpha subunit, Gi alpha 1. The switch II and switch III segments become disordered, and linker II connecting the Ras and alpha helical domains moves, thus altering the structures of potential effector and beta gamma binding regions. Contacts between the alpha-helical and Ras domains are weakened, possibly facilitating the release of guanosine diphosphate (GDP). The amino and carboxyl termini, which contain receptor and beta gamma binding determinants, are disordered in the complex with GTP, but are organized into a compact microdomain on GDP hydrolysis. The amino terminus also forms extensive quaternary contacts with neighboring alpha subunits in the lattice, suggesting that multimers of alpha subunits or heterotrimers may play a role in signal transduction.

PubMed: 7481799

実験手法

X-RAY DIFFRACTION (2.2 Å)