1U90

Crystal structures of Ral-GppNHp and Ral-GDP reveal two novel binding sites that are also present in Ras and Rap

1U90 の概要

• エントリーDOI: 10.2210/pdb1u90/pdb
• 関連するPDBエントリー: 1U8Y 1U8Z
• 分子名称: Ras-related protein Ral-A, MAGNESIUM ION, GUANOSINE-5'-DIPHOSPHATE, ... (4 entities in total)
• 機能のキーワード: ral, gtpase, ras, gdp, gtp, gnp, gmppnp, gppnhp, signaling protein
• 由来する生物種: Saguinus oedipus (cotton-top tamarin)
• 細胞内の位置: Cell membrane ; Lipid-anchor ; Cytoplasmic side : P63320
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 39287.92

構造登録者

Nicely, N.I.,Kosak, J.,de Serrano, V.,Mattos, C. (登録日: 2004-08-09, 公開日: 2004-11-23, 最終更新日: 2023-08-23)

主引用文献

Nicely, N.I.,Kosak, J.,de Serrano, V.,Mattos, C.
Crystal Structures of Ral-GppNHp and Ral-GDP Reveal Two Binding Sites that Are Also Present in Ras and Rap
Structure, 12:2025-2036, 2004

PubMed Abstract: RalA is a GTPase with effectors such as Sec5 and Exo84 in the exocyst complex and RalBP1, a GAP for Rho proteins. We report the crystal structures of Ral-GppNHp and Ral-GDP. Disordered switch I and switch II, located away from crystal contacts, are observed in one of the molecules in the asymmetric unit of the Ral-GppNHp structure. In the other molecule in the asymmetric unit, a second Mg(2+) ion is bound to the GppNHp gamma-phosphate in an environment in which switch I is pulled away from the nucleotide and switch II is found in a tight beta turn. Clustering of conserved residues on the surface of Ral-GppNHp identifies two putative sites for protein-protein interaction. One site is adjacent to switch I. The other is modulated by switch II and is obstructed in Ral-GDP. The Ral structures are discussed in the context of the published structures of the Ral/Sec5 complex, Ras, and Rap.

PubMed: 15530367
DOI: 10.1016/j.str.2004.08.011

実験手法

X-RAY DIFFRACTION (2 Å)