1fqk
From Proteopedia
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|PDB= 1fqk |SIZE=350|CAPTION= <scene name='initialview01'>1fqk</scene>, resolution 2.30Å | |PDB= 1fqk |SIZE=350|CAPTION= <scene name='initialview01'>1fqk</scene>, resolution 2.30Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=ALF:TETRAFLUOROALUMINATE+ION'>ALF</scene>, <scene name='pdbligand=GDP:GUANOSINE-5'-DIPHOSPHATE'>GDP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1fqj|1FQJ]], [[1fqi|1fqi]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1fqk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fqk OCA], [http://www.ebi.ac.uk/pdbsum/1fqk PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1fqk RCSB]</span> | ||
}} | }} | ||
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[[Category: Slep, K C.]] | [[Category: Slep, K C.]] | ||
[[Category: Wensel, T G.]] | [[Category: Wensel, T G.]] | ||
| - | [[Category: ALF]] | ||
| - | [[Category: GDP]] | ||
| - | [[Category: MG]] | ||
[[Category: g protein]] | [[Category: g protein]] | ||
[[Category: gap]] | [[Category: gap]] | ||
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[[Category: transducin]] | [[Category: transducin]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:28:21 2008'' |
Revision as of 17:28, 30 March 2008
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| , resolution 2.30Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , | ||||||
| Related: | 1FQJ, 1fqi
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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 Sun Mar 30 20:28:21 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. | G protein | Gap | Phototransduction | Rg | Rgs9 | Rod | Transducin
