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spinqualitylabelsall models 1fqi, resolution 1.94Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

RGS9 RGS DOMAIN

Overview

A multitude of heptahelical receptors use heterotrimeric G proteins to, transduce signals to specific effector target molecules. The G protein, transducin, Gt, couples photon-activated rhodopsin with the effector, cyclic GMP phosophodiesterase (PDE) in the vertebrate phototransduction, cascade. The interactions of the Gt alpha-subunit (alpha(t)) with the, inhibitory PDE gamma-subunit (PDEgamma) are central to effector, activation, and also enhance visual recovery in cooperation with the, GTPase-activating protein regulator of G-protein signalling (RGS)-9 (refs, 1-3). Here we describe the crystal structure at 2.0 A of rod transducin, alpha x GDP x AlF4- in complex with the effector molecule PDEgamma and the, GTPase-activating protein RGS9. In addition, we present the independently, solved crystal structures of the RGS9 RGS domain both alone and in complex, with alpha(t/i1) x GDP x AlF4-. These structures reveal insights into, effector activation, synergistic GTPase acceleration, RGS9 specificity and, RGS activity. Effector binding to a nucleotide-dependent site on alpha(t), sequesters PDEgamma residues implicated in PDE inhibition, and potentiates, recruitment of RGS9 for hydrolytic transition state stabilization and, concomitant signal termination.

About this Structure

1FQI is a Single protein structure of sequence from Bos taurus. Full crystallographic information is available from OCA.

Reference

Structural determinants for regulation of phosphodiesterase by a G protein at 2.0 A., Slep KC, Kercher MA, He W, Cowan CW, Wensel TG, Sigler PB, Nature. 2001 Feb 22;409(6823):1071-7. PMID:11234020

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