1gdd: Difference between revisions

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New page: left|200px<br /><applet load="1gdd" size="450" color="white" frame="true" align="right" spinBox="true" caption="1gdd, resolution 2.2Å" /> '''TERTIARY AND QUATERNA...
 
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'''TERTIARY AND QUATERNARY STRUCTURAL CHANGES IN GIA1 INDUCED BY GTP HYDROLYSIS'''<br />


==Overview==
==TERTIARY AND QUATERNARY STRUCTURAL CHANGES IN GIA1 INDUCED BY GTP HYDROLYSIS==
Crystallographic analysis of 2.2 angstrom resolution shows that guanosine, triphosphate (GTP) hydrolysis triggers conformational changes in the, heterotrimeric G-protein alpha subunit, Gi alpha 1. The switch II and, switch III segments become disordered, and linker II connecting the Ras, and alpha helical domains moves, thus altering the structures of potential, effector and beta gamma binding regions. Contacts between the, alpha-helical and Ras domains are weakened, possibly facilitating the, release of guanosine diphosphate (GDP). The amino and carboxyl termini, which contain receptor and beta gamma binding determinants, are disordered, in the complex with GTP, but are organized into a compact microdomain on, GDP hydrolysis. The amino terminus also forms extensive quaternary, contacts with neighboring alpha subunits in the lattice, suggesting that, multimers of alpha subunits or heterotrimers may play a role in signal, transduction.
<StructureSection load='1gdd' size='340' side='right'caption='[[1gdd]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
 
== Structural highlights ==
==About this Structure==
<table><tr><td colspan='2'>[[1gdd]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GDD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1GDD FirstGlance]. <br>
1GDD is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] with SO4 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=1GDD OCA].  
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2&#8491;</td></tr>
 
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GDP:GUANOSINE-5-DIPHOSPHATE'>GDP</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
==Reference==
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1gdd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gdd OCA], [https://pdbe.org/1gdd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1gdd RCSB], [https://www.ebi.ac.uk/pdbsum/1gdd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1gdd ProSAT]</span></td></tr>
Tertiary and quaternary structural changes in Gi alpha 1 induced by GTP hydrolysis., Mixon MB, Lee E, Coleman DE, Berghuis AM, Gilman AG, Sprang SR, Science. 1995 Nov 10;270(5238):954-60. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=7481799 7481799]
</table>
== Function ==
[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/gd/1gdd_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=1gdd ConSurf].
<div style="clear:both"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Rattus norvegicus]]
[[Category: Rattus norvegicus]]
[[Category: Single protein]]
[[Category: Mixon MB]]
[[Category: Mixon, M.B.]]
[[Category: Sprang SR]]
[[Category: Sprang, S.R.]]
[[Category: GDP]]
[[Category: SO4]]
[[Category: gtp-ase]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 15:57:45 2007''

Latest revision as of 10:24, 7 February 2024

TERTIARY AND QUATERNARY STRUCTURAL CHANGES IN GIA1 INDUCED BY GTP HYDROLYSISTERTIARY AND QUATERNARY STRUCTURAL CHANGES IN GIA1 INDUCED BY GTP HYDROLYSIS

Structural highlights

1gdd is a 1 chain structure with sequence from Rattus norvegicus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.2Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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.

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

1gdd, resolution 2.20Å

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