1u90

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spinqualitylabelsall models 1u90, resolution 2.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

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

Overview

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.

About this Structure

1U90 is a Single protein structure of sequence from Saguinus oedipus with MG and GDP as ligands. Full crystallographic information is available from OCA.

Reference

Crystal structures of Ral-GppNHp and Ral-GDP reveal two binding sites that are also present in Ras and Rap., Nicely NI, Kosak J, de Serrano V, Mattos C, Structure. 2004 Nov;12(11):2025-36. PMID:15530367

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