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New page: left|200px<br /><applet load="1fqj" size="450" color="white" frame="true" align="right" spinBox="true" caption="1fqj, resolution 2.02Å" /> '''CRYSTAL STRUCTURE OF...
 
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[[Image:1fqj.gif|left|200px]]<br /><applet load="1fqj" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1fqj.gif|left|200px]]<br /><applet load="1fqj" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1fqj, resolution 2.02&Aring;" />
caption="1fqj, resolution 2.02&Aring;" />
'''CRYSTAL STRUCTURE OF THE HETEROTRIMERIC COMPLEX OF THE RGS DOMAIN OF RGS9, THE GAMMA SUBUNIT OF PHOSPHODIESTERASE AND THE GT/I1 CHIMERA ALPHA SUBUNIT [(RGS9)-(PDEGAMMA)-(GT/I1ALPHA)-(GDP)-(ALF4-)-(MG2+)]'''<br />
'''CRYSTAL STRUCTURE OF THE HETEROTRIMERIC COMPLEX OF THE RGS DOMAIN OF RGS9, THE GAMMA SUBUNIT OF PHOSPHODIESTERASE AND THE GT/I1 CHIMERA ALPHA SUBUNIT [(RGS9)-(PDEGAMMA)-(GT/I1ALPHA)-(GDP)-(ALF4-)-(MG2+)]'''<br />


==Overview==
==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.
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==
1FQJ 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]. Active as [http://en.wikipedia.org/wiki/3',5'-cyclic-nucleotide_phosphodiesterase 3',5'-cyclic-nucleotide phosphodiesterase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.4.17 3.1.4.17] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1FQJ OCA].  
1FQJ 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]. Active as [http://en.wikipedia.org/wiki/3',5'-cyclic-nucleotide_phosphodiesterase 3',5'-cyclic-nucleotide phosphodiesterase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.4.17 3.1.4.17] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FQJ 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.W.]]
[[Category: Cowan, C W.]]
[[Category: He, W.]]
[[Category: He, W.]]
[[Category: Kercher, M.A.]]
[[Category: Kercher, M A.]]
[[Category: Sigler, P.B.]]
[[Category: Sigler, P B.]]
[[Category: Slep, K.C.]]
[[Category: Slep, K C.]]
[[Category: Wensel, T.G.]]
[[Category: Wensel, T G.]]
[[Category: ALF]]
[[Category: ALF]]
[[Category: GDP]]
[[Category: GDP]]
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[[Category: transducin]]
[[Category: transducin]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 15:09:58 2007''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:41:33 2008''