1svk

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[[Image:1svk.gif|left|200px]]<br /><applet load="1svk" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1svk.gif|left|200px]]
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caption="1svk, resolution 2.00&Aring;" />
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'''Structure of the K180P mutant of Gi alpha subunit bound to AlF4 and GDP'''<br />
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{{Structure
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|PDB= 1svk |SIZE=350|CAPTION= <scene name='initialview01'>1svk</scene>, resolution 2.00&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=ALF:TETRAFLUOROALUMINATE+ION'>ALF</scene> and <scene name='pdbligand=GDP:GUANOSINE-5'-DIPHOSPHATE'>GDP</scene>
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|ACTIVITY= [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]
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|GENE= GNAI1, GNAI-1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Rattus norvegicus])
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}}
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'''Structure of the K180P mutant of Gi alpha subunit bound to AlF4 and GDP'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1SVK 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 <scene name='pdbligand=MG:'>MG</scene>, <scene name='pdbligand=ALF:'>ALF</scene> and <scene name='pdbligand=GDP:'>GDP</scene> 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://oca.weizmann.ac.il/oca-bin/ocashort?id=1SVK OCA].
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1SVK is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SVK OCA].
==Reference==
==Reference==
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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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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://www.ncbi.nlm.nih.gov/pubmed/15128951 15128951]
[[Category: Heterotrimeric G-protein GTPase]]
[[Category: Heterotrimeric G-protein GTPase]]
[[Category: Rattus norvegicus]]
[[Category: Rattus norvegicus]]
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[[Category: k180p mutation]]
[[Category: k180p mutation]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:05:38 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:10:12 2008''

Revision as of 12:10, 20 March 2008

Image:1svk.gif


PDB ID 1svk

Drag the structure with the mouse to rotate
, resolution 2.00Å
Ligands: , and
Gene: GNAI1, GNAI-1 (Rattus norvegicus)
Activity: Heterotrimeric G-protein GTPase, with EC number 3.6.5.1
Coordinates: save as pdb, mmCIF, xml



Structure of the K180P mutant of Gi alpha subunit bound to AlF4 and GDP


Overview

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-->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-->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.

About this Structure

1SVK is a Single protein structure of sequence from Rattus norvegicus. Full crystallographic information is available from OCA.

Reference

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:15128951

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