1fqj
From Proteopedia
(Difference between revisions)
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<StructureSection load='1fqj' size='340' side='right'caption='[[1fqj]], [[Resolution|resolution]] 2.02Å' scene=''> | <StructureSection load='1fqj' size='340' side='right'caption='[[1fqj]], [[Resolution|resolution]] 2.02Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
- | <table><tr><td colspan='2'>[[1fqj]] is a 5 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FQJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FQJ FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1fqj]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus] and [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FQJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FQJ FirstGlance]. <br> |
- | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.02Å</td></tr> |
- | <tr id=' | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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></td></tr> |
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1fqj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fqj OCA], [https://pdbe.org/1fqj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1fqj RCSB], [https://www.ebi.ac.uk/pdbsum/1fqj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1fqj ProSAT]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1fqj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fqj OCA], [https://pdbe.org/1fqj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1fqj RCSB], [https://www.ebi.ac.uk/pdbsum/1fqj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1fqj ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
- | + | [https://www.uniprot.org/uniprot/GNAT1_BOVIN GNAT1_BOVIN] Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems. Transducin is an amplifier and one of the transducers of a visual impulse that performs the coupling between rhodopsin and cGMP-phosphodiesterase.[https://www.uniprot.org/uniprot/GNAI1_RAT GNAI1_RAT] Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems. The G(i) proteins are involved in hormonal regulation of adenylate cyclase: they inhibit the cyclase in response to beta-adrenergic stimuli. The inactive GDP-bound form prevents the association of RGS14 with centrosomes and is required for the translocation of RGS14 from the cytoplasm to the plasma membrane. May play a role in cell division.<ref>PMID:16870394</ref> | |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1fqj ConSurf]. | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1fqj ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
- | <div style="background-color:#fffaf0;"> | ||
- | == Publication Abstract from PubMed == | ||
- | 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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- | 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<ref>PMID:11234020</ref> | ||
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- | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
- | </div> | ||
- | <div class="pdbe-citations 1fqj" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
- | [[Category: | + | [[Category: Bos taurus]] |
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
- | [[Category: Cowan | + | [[Category: Rattus norvegicus]] |
- | [[Category: He | + | [[Category: Cowan CW]] |
- | [[Category: Kercher | + | [[Category: He W]] |
- | [[Category: Sigler | + | [[Category: Kercher MA]] |
- | [[Category: Slep | + | [[Category: Sigler PB]] |
- | [[Category: Wensel | + | [[Category: Slep KC]] |
- | + | [[Category: Wensel TG]] | |
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Current revision
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+)]
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Categories: Bos taurus | Large Structures | Rattus norvegicus | Cowan CW | He W | Kercher MA | Sigler PB | Slep KC | Wensel TG