1zcb: Difference between revisions
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[[Image:1zcb.gif|left|200px]] | [[Image:1zcb.gif|left|200px]] | ||
'''Crystal structure of G alpha 13 in complex with GDP''' | {{Structure | ||
|PDB= 1zcb |SIZE=350|CAPTION= <scene name='initialview01'>1zcb</scene>, resolution 2.00Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=GDP:GUANOSINE-5'-DIPHOSPHATE'>GDP</scene> | |||
|ACTIVITY= | |||
|GENE= | |||
}} | |||
'''Crystal structure of G alpha 13 in complex with GDP''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1ZCB is a [ | 1ZCB is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZCB OCA]. | ||
==Reference== | ==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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/16388592 16388592] | ||
[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: transducer]] | [[Category: transducer]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 15:33:44 2008'' | ||
Revision as of 13:33, 20 March 2008
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| 1zcb, resolution 2.00Å | |||||||||||||
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| Ligands: | GDP | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
Crystal structure of G alpha 13 in complex with GDP
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
1ZCB is a Single protein structure of sequence from Mus musculus. 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
Page seeded by OCA on Thu Mar 20 15:33:44 2008
