1zcb: Difference between revisions

Line 1:

[[Image:1zcb.gif|left|200px]]<br /><applet load="1zcb" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

[[Image:1zcb.gif|left|200px]]<br /><applet load="1zcb" size="350" color="white" frame="true" align="right" spinBox="true"

caption="1zcb, resolution 2.00Å" />

'''Crystal structure of G alpha 13 in complex with GDP'''<br />

==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.

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==

1ZCB 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 GDP as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=1ZCB OCA].

1ZCB 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=GDP:'>GDP</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZCB OCA].

==Reference==

Line 13:

[[Category: Mus musculus]]

[[Category: Single protein]]

[[Category: Nance, M.R.]]

[[Category: Nance, M R.]]

[[Category: Tesmer, J.J.G.]]

[[Category: Tesmer, J J.G.]]

[[Category: GDP]]

[[Category: gtp-binding]]

Line 21:

[[Category: transducer]]

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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:14:10 2008''

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@@ Line 1: / Line 1: @@
-[[Image:1zcb.gif|left|200px]]<br /><applet load="1zcb" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1zcb.gif|left|200px]]<br /><applet load="1zcb" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1zcb, resolution 2.00&Aring;" />
 '''Crystal structure of G alpha 13 in complex with GDP'''<br />
 ==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.
+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==
-ZCB 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 GDP as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1ZCB OCA].
+ZCB 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=GDP:'>GDP</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZCB OCA].
 ==Reference==
@@ Line 13: / Line 13: @@
 [[Category: Mus musculus]]
 [[Category: Single protein]]
-[[Category: Nance, M.R.]]
+[[Category: Nance, M R.]]
-[[Category: Tesmer, J.J.G.]]
+[[Category: Tesmer, J J.G.]]
 [[Category: GDP]]
 [[Category: gtp-binding]]
@@ Line 21: / Line 21: @@
 [[Category: transducer]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 07:22:52 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:14:10 2008''