1fqi

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(New page: 200px<br /><applet load="1fqi" size="450" color="white" frame="true" align="right" spinBox="true" caption="1fqi, resolution 1.94&Aring;" /> '''RGS9 RGS DOMAIN'''<b...)
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[[Image:1fqi.gif|left|200px]]<br /><applet load="1fqi" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1fqi.gif|left|200px]]<br /><applet load="1fqi" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1fqi, resolution 1.94&Aring;" />
caption="1fqi, resolution 1.94&Aring;" />
'''RGS9 RGS DOMAIN'''<br />
'''RGS9 RGS DOMAIN'''<br />
==Overview==
==Overview==
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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.
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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==
==About this Structure==
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1FQI is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1FQI OCA].
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1FQI is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FQI OCA].
==Reference==
==Reference==
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[[Category: Bos taurus]]
[[Category: Bos taurus]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Cowan, C.W.]]
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[[Category: Cowan, C W.]]
[[Category: He, W.]]
[[Category: He, W.]]
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[[Category: Kercher, M.A.]]
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[[Category: Kercher, M A.]]
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[[Category: Sigler, P.B.]]
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[[Category: Sigler, P B.]]
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[[Category: Slep, K.C.]]
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[[Category: Slep, K C.]]
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[[Category: Wensel, T.G.]]
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[[Category: Wensel, T G.]]
[[Category: gap]]
[[Category: gap]]
[[Category: phototransduction]]
[[Category: phototransduction]]
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[[Category: rod]]
[[Category: rod]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 15:09:52 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:41:33 2008''

Revision as of 10:41, 21 February 2008


1fqi, resolution 1.94Å

Drag the structure with the mouse to rotate

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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