1U8Y

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

Summary for 1U8Y

• Entry DOI: 10.2210/pdb1u8y/pdb
• Related: 1U8Z 1U90
• Descriptor: Ras-related protein Ral-A, MAGNESIUM ION, PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER, ... (4 entities in total)
• Functional Keywords: signaling protein
• Biological source: Saguinus oedipus (cotton-top tamarin)
• Cellular location: Cell surface (By similarity): P63320
• Total number of polymer chains: 2
• Total formula weight: 39494.52

Authors

Nicely, N.I.,Kosak, J.,de Serrano, V.,Mattos, C. (deposition date: 2004-08-09, release date: 2004-11-23, Last modification date: 2024-02-14)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (1.55 Å)