1fqi: Difference between revisions
New page: left|200px<br /><applet load="1fqi" size="450" color="white" frame="true" align="right" spinBox="true" caption="1fqi, resolution 1.94Å" /> '''RGS9 RGS DOMAIN'''<b... |
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[[Image:1fqi.gif|left|200px]]<br /><applet load="1fqi" size=" | [[Image:1fqi.gif|left|200px]]<br /><applet load="1fqi" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1fqi, resolution 1.94Å" /> | caption="1fqi, resolution 1.94Å" /> | ||
'''RGS9 RGS DOMAIN'''<br /> | '''RGS9 RGS DOMAIN'''<br /> | ||
==Overview== | ==Overview== | ||
A multitude of heptahelical receptors use heterotrimeric G proteins to | 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== | ||
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:// | 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]] | ||
[[Category: Cowan, C | [[Category: Cowan, C W.]] | ||
[[Category: He, W.]] | [[Category: He, W.]] | ||
[[Category: Kercher, M | [[Category: Kercher, M A.]] | ||
[[Category: Sigler, P | [[Category: Sigler, P B.]] | ||
[[Category: Slep, K | [[Category: Slep, K C.]] | ||
[[Category: Wensel, T | [[Category: Wensel, T G.]] | ||
[[Category: gap]] | [[Category: gap]] | ||
[[Category: phototransduction]] | [[Category: phototransduction]] | ||
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[[Category: rod]] | [[Category: rod]] | ||
''Page seeded by [http:// | ''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
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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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