1fqk
From Proteopedia
(New page: 200px<br /><applet load="1fqk" size="450" color="white" frame="true" align="right" spinBox="true" caption="1fqk, resolution 2.30Å" /> '''CRYSTAL STRUCTURE OF...) |
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| - | [[Image:1fqk.jpg|left|200px]]<br /><applet load="1fqk" size=" | + | [[Image:1fqk.jpg|left|200px]]<br /><applet load="1fqk" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1fqk, resolution 2.30Å" /> | caption="1fqk, resolution 2.30Å" /> | ||
'''CRYSTAL STRUCTURE OF THE HETERODIMERIC COMPLEX OF THE RGS DOMAIN OF RGS9, AND THE GT/I1 CHIMERA ALPHA SUBUNIT [(RGS9)-(GT/I1ALPHA)-(GDP)-(ALF4-)-(MG2+)]'''<br /> | '''CRYSTAL STRUCTURE OF THE HETERODIMERIC COMPLEX OF THE RGS DOMAIN OF RGS9, AND THE GT/I1 CHIMERA ALPHA SUBUNIT [(RGS9)-(GT/I1ALPHA)-(GDP)-(ALF4-)-(MG2+)]'''<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== | ||
| - | 1FQK is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Bos_taurus_and_rattus_norvegicus Bos taurus and rattus norvegicus] and [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] with MG, ALF and GDP as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1FQK is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Bos_taurus_and_rattus_norvegicus Bos taurus and rattus norvegicus] and [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] with <scene name='pdbligand=MG:'>MG</scene>, <scene name='pdbligand=ALF:'>ALF</scene> and <scene name='pdbligand=GDP:'>GDP</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FQK OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Bos taurus and rattus norvegicus]] | [[Category: Bos taurus and rattus norvegicus]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
| - | [[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: ALF]] | [[Category: ALF]] | ||
[[Category: GDP]] | [[Category: GDP]] | ||
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[[Category: transducin]] | [[Category: transducin]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:41:37 2008'' |
Revision as of 10:41, 21 February 2008
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CRYSTAL STRUCTURE OF THE HETERODIMERIC COMPLEX OF THE RGS DOMAIN OF RGS9, AND THE GT/I1 CHIMERA ALPHA SUBUNIT [(RGS9)-(GT/I1ALPHA)-(GDP)-(ALF4-)-(MG2+)]
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
1FQK is a Protein complex structure of sequences from Bos taurus and rattus norvegicus and Bos taurus with , and as ligands. 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
Page seeded by OCA on Thu Feb 21 12:41:37 2008
Categories: Bos taurus | Bos taurus and rattus norvegicus | Protein complex | Cowan, C W. | He, W. | Kercher, M A. | Sigler, P B. | Slep, K C. | Wensel, T G. | ALF | GDP | MG | G protein | Gap | Phototransduction | Rgs | Rgs9 | Rod | Transducin
