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1svs

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(New page: 200px<br /><applet load="1svs" size="450" color="white" frame="true" align="right" spinBox="true" caption="1svs, resolution 1.5&Aring;" /> '''Structure of the K180...)
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[[Image:1svs.jpg|left|200px]]<br /><applet load="1svs" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1svs, resolution 1.5&Aring;" />
 
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'''Structure of the K180P mutant of Gi alpha subunit bound to GppNHp.'''<br />
 
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==Overview==
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==Structure of the K180P mutant of Gi alpha subunit bound to GppNHp.==
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Heterotrimeric G protein alpha (G alpha) subunits possess intrinsic GTPase, activity that leads to functional deactivation with a rate constant of, approximately 2 min(-1) at 30 degrees C. GTP hydrolysis causes, conformational changes in three regions of G alpha, including Switch I and, Switch II. Mutation of G202--&gt;A in Switch II of G alpha(i1) accelerates, the rates of both GTP hydrolysis and conformational change, which is, measured by the loss of fluorescence from Trp-211 in Switch II. Mutation, of K180--&gt;P in Switch I increases the rate of conformational change but, decreases the GTPase rate, which causes transient but substantial, accumulation of a low-fluorescence G alpha(i1).GTP species. Isothermal, titration calorimetric analysis of the binding of (G202A)G alpha(i1) and, (K180P)G alpha(i1) to the GTPase-activating protein RGS4 indicates that, the G202A mutation stabilizes the pretransition state-like conformation of, G alpha(i1) that is mimicked by the complex of G alpha(i1) with GDP and, magnesium fluoroaluminate, whereas the K180P mutation destabilizes this, state. The crystal structures of (K180P)G alpha(i1) bound to a slowly, hydrolyzable GTP analog, and the GDP.magnesium fluoroaluminate complex, provide evidence that the Mg(2+) binding site is destabilized and that, Switch I is torsionally restrained by the K180P mutation. The data are, consistent with a catalytic mechanism for G alpha in which major, conformational transitions in Switch I and Switch II are obligate events, that precede the bond-breaking step in GTP hydrolysis. In (K180P)G, alpha(i1), the two events are decoupled kinetically, whereas in the native, protein they are concerted.
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<StructureSection load='1svs' size='340' side='right'caption='[[1svs]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
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== Structural highlights ==
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==About this Structure==
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<table><tr><td colspan='2'>[[1svs]] 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=1SVS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1SVS FirstGlance]. <br>
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1SVS 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 MG and GNP as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Heterotrimeric_G-protein_GTPase Heterotrimeric G-protein GTPase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.5.1 3.6.5.1] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1SVS OCA].
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.5&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GNP:PHOSPHOAMINOPHOSPHONIC+ACID-GUANYLATE+ESTER'>GNP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
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==Reference==
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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=1svs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1svs OCA], [https://pdbe.org/1svs PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1svs RCSB], [https://www.ebi.ac.uk/pdbsum/1svs PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1svs ProSAT]</span></td></tr>
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Uncoupling conformational change from GTP hydrolysis in a heterotrimeric G protein alpha-subunit., Thomas CJ, Du X, Li P, Wang Y, Ross EM, Sprang SR, Proc Natl Acad Sci U S A. 2004 May 18;101(20):7560-5. Epub 2004 May 5. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15128951 15128951]
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</table>
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[[Category: Heterotrimeric G-protein GTPase]]
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== Function ==
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[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>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/sv/1svs_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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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=1svs ConSurf].
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<div style="clear:both"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
[[Category: Rattus norvegicus]]
[[Category: Rattus norvegicus]]
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[[Category: Single protein]]
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[[Category: Du X]]
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[[Category: Du, X.]]
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[[Category: Li P]]
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[[Category: Li, P.]]
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[[Category: Ross EM]]
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[[Category: Ross, E.M.]]
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[[Category: Sprang SR]]
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[[Category: Sprang, S.R.]]
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[[Category: Thomas CJ]]
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[[Category: Thomas, C.J.]]
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[[Category: Wang Y]]
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[[Category: Wang, Y.]]
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[[Category: GNP]]
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[[Category: MG]]
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[[Category: gi alpha subunit]]
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[[Category: gppnhp (gnp) bound]]
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[[Category: k180p mutation]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 02:46:12 2007''
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Current revision

Structure of the K180P mutant of Gi alpha subunit bound to GppNHp.

PDB ID 1svs

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