1zca

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(New page: 200px<br /><applet load="1zca" size="450" color="white" frame="true" align="right" spinBox="true" caption="1zca, resolution 2.9&Aring;" /> '''Crystal structure of ...)
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[[Image:1zca.gif|left|200px]]<br /><applet load="1zca" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1zca.gif|left|200px]]<br /><applet load="1zca" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1zca, resolution 2.9&Aring;" />
caption="1zca, resolution 2.9&Aring;" />
'''Crystal structure of G alpha 12 in complex with GDP, Mg2+ and AlF4-'''<br />
'''Crystal structure of G alpha 12 in complex with GDP, Mg2+ and AlF4-'''<br />
==Overview==
==Overview==
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The oncogenic G(12/13) subfamily of heterotrimeric G proteins transduces, extracellular signals that regulate the actin cytoskeleton, cell cycle, progression, and gene transcription. Previously, structural analyses of, fully functional G alpha(12/13) subunits have been hindered by, insufficient amounts of homogeneous, functional protein. Herein, we report, that substitution of the N-terminal helix of G alpha(i1) for the, corresponding region of G alpha12 or G alpha13 generated soluble chimeric, subunits (G alpha(i/12) and G alpha(i/13)) that could be purified in, sufficient amounts for crystallographic studies. Each chimera bound, guanine nucleotides, G betagamma subunits, and effector proteins and, exhibited GAP responses to p115RhoGEF and leukemia-associated RhoGEF. Like, their wild-type counterparts, G alpha(i/13), but not G alpha(i/12), stimulated the activity of p115RhoGEF. Crystal structures of the G, alpha(i/12) x GDP x AlF4(-) and G alpha(i/13) x GDP complexes were, determined using diffraction data extending to 2.9 and 2.0 A, respectively. These structures reveal not only the native structural, features of G alpha12 and G alpha13 subunits, which are expected to be, important for their interactions with GPCRs and effectors such as G, alpha-regulated RhoGEFs, but also novel conformational changes that are, likely coupled to GTP hydrolysis in the G alpha(12/13) class of, heterotrimeric G proteins.
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The oncogenic G(12/13) subfamily of heterotrimeric G proteins transduces extracellular signals that regulate the actin cytoskeleton, cell cycle progression, and gene transcription. Previously, structural analyses of fully functional G alpha(12/13) subunits have been hindered by insufficient amounts of homogeneous, functional protein. Herein, we report that substitution of the N-terminal helix of G alpha(i1) for the corresponding region of G alpha12 or G alpha13 generated soluble chimeric subunits (G alpha(i/12) and G alpha(i/13)) that could be purified in sufficient amounts for crystallographic studies. Each chimera bound guanine nucleotides, G betagamma subunits, and effector proteins and exhibited GAP responses to p115RhoGEF and leukemia-associated RhoGEF. Like their wild-type counterparts, G alpha(i/13), but not G alpha(i/12), stimulated the activity of p115RhoGEF. Crystal structures of the G alpha(i/12) x GDP x AlF4(-) and G alpha(i/13) x GDP complexes were determined using diffraction data extending to 2.9 and 2.0 A, respectively. These structures reveal not only the native structural features of G alpha12 and G alpha13 subunits, which are expected to be important for their interactions with GPCRs and effectors such as G alpha-regulated RhoGEFs, but also novel conformational changes that are likely coupled to GTP hydrolysis in the G alpha(12/13) class of heterotrimeric G proteins.
==About this Structure==
==About this Structure==
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1ZCA is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] 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=1ZCA OCA].
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1ZCA is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] 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]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZCA OCA].
==Reference==
==Reference==
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[[Category: Mus musculus]]
[[Category: Mus musculus]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Nance, M.R.]]
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[[Category: Nance, M R.]]
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[[Category: Tesmer, J.J.G.]]
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[[Category: Tesmer, J J.G.]]
[[Category: ALF]]
[[Category: ALF]]
[[Category: GDP]]
[[Category: GDP]]
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[[Category: transducer]]
[[Category: transducer]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 07:22:49 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:14:08 2008''

Revision as of 14:14, 21 February 2008


1zca, resolution 2.9Å

Drag the structure with the mouse to rotate

Crystal structure of G alpha 12 in complex with GDP, Mg2+ and AlF4-

Overview

The oncogenic G(12/13) subfamily of heterotrimeric G proteins transduces extracellular signals that regulate the actin cytoskeleton, cell cycle progression, and gene transcription. Previously, structural analyses of fully functional G alpha(12/13) subunits have been hindered by insufficient amounts of homogeneous, functional protein. Herein, we report that substitution of the N-terminal helix of G alpha(i1) for the corresponding region of G alpha12 or G alpha13 generated soluble chimeric subunits (G alpha(i/12) and G alpha(i/13)) that could be purified in sufficient amounts for crystallographic studies. Each chimera bound guanine nucleotides, G betagamma subunits, and effector proteins and exhibited GAP responses to p115RhoGEF and leukemia-associated RhoGEF. Like their wild-type counterparts, G alpha(i/13), but not G alpha(i/12), stimulated the activity of p115RhoGEF. Crystal structures of the G alpha(i/12) x GDP x AlF4(-) and G alpha(i/13) x GDP complexes were determined using diffraction data extending to 2.9 and 2.0 A, respectively. These structures reveal not only the native structural features of G alpha12 and G alpha13 subunits, which are expected to be important for their interactions with GPCRs and effectors such as G alpha-regulated RhoGEFs, but also novel conformational changes that are likely coupled to GTP hydrolysis in the G alpha(12/13) class of heterotrimeric G proteins.

About this Structure

1ZCA is a Single protein structure of sequence from Mus musculus with , and as ligands. Full crystallographic information is available from OCA.

Reference

A new approach to producing functional G alpha subunits yields the activated and deactivated structures of G alpha(12/13) proteins., Kreutz B, Yau DM, Nance MR, Tanabe S, Tesmer JJ, Kozasa T, Biochemistry. 2006 Jan 10;45(1):167-74. PMID:16388592

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