1fqk: Difference between revisions

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New page: left|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="450" color="white" frame="true" align="right" spinBox="true"
caption="1fqk, resolution 2.30&Aring;" />
'''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==
==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+)]==
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.
<StructureSection load='1fqk' size='340' side='right'caption='[[1fqk]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1fqk]] is a 4 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=1FQK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FQK FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3&#8491;</td></tr>
<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>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1fqk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fqk OCA], [https://pdbe.org/1fqk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1fqk RCSB], [https://www.ebi.ac.uk/pdbsum/1fqk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1fqk ProSAT]</span></td></tr>
</table>
== 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 ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fq/1fqk_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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=1fqk ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1FQK OCA].
*[[Regulator of G-protein signaling 3D structures|Regulator of G-protein signaling 3D structures]]
 
*[[Transducin 3D structures|Transducin 3D structures]]
==Reference==
== References ==
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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11234020 11234020]
<references/>
__TOC__
</StructureSection>
[[Category: Bos taurus]]
[[Category: Bos taurus]]
[[Category: Bos taurus and rattus norvegicus]]
[[Category: Large Structures]]
[[Category: Protein complex]]
[[Category: Rattus norvegicus]]
[[Category: Cowan, C.W.]]
[[Category: Cowan CW]]
[[Category: He, W.]]
[[Category: He W]]
[[Category: Kercher, M.A.]]
[[Category: Kercher MA]]
[[Category: Sigler, P.B.]]
[[Category: Sigler PB]]
[[Category: Slep, K.C.]]
[[Category: Slep KC]]
[[Category: Wensel, T.G.]]
[[Category: Wensel TG]]
[[Category: ALF]]
[[Category: GDP]]
[[Category: MG]]
[[Category: g protein]]
[[Category: gap]]
[[Category: phototransduction]]
[[Category: rgs]]
[[Category: rgs9]]
[[Category: rod]]
[[Category: transducin]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 15:10:08 2007''

Latest revision as of 10:17, 7 February 2024

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+)]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+)]

Structural highlights

1fqk is a 4 chain structure with sequence from Bos taurus and Rattus norvegicus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.3Å
Ligands:, ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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.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.[1]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

References

  1. ↑ Shu FJ, Ramineni S, Amyot W, Hepler JR. Selective interactions between Gi alpha1 and Gi alpha3 and the GoLoco/GPR domain of RGS14 influence its dynamic subcellular localization. Cell Signal. 2007 Jan;19(1):163-76. Epub 2006 Jul 25. PMID:16870394 doi:http://dx.doi.org/10.1016/j.cellsig.2006.06.002

1fqk, resolution 2.30Å

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