1zca
From Proteopedia
| Line 4: | Line 4: | ||
|PDB= 1zca |SIZE=350|CAPTION= <scene name='initialview01'>1zca</scene>, resolution 2.9Å | |PDB= 1zca |SIZE=350|CAPTION= <scene name='initialview01'>1zca</scene>, resolution 2.9Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=ALF:TETRAFLUOROALUMINATE+ION'>ALF</scene>, <scene name='pdbligand=GDP:GUANOSINE-5'-DIPHOSPHATE'>GDP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1zcb|1ZCB]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1zca FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1zca OCA], [http://www.ebi.ac.uk/pdbsum/1zca PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1zca RCSB]</span> | ||
}} | }} | ||
| Line 24: | Line 27: | ||
[[Category: Nance, M R.]] | [[Category: Nance, M R.]] | ||
[[Category: Tesmer, J J.G.]] | [[Category: Tesmer, J J.G.]] | ||
| - | [[Category: ALF]] | ||
| - | [[Category: GDP]] | ||
| - | [[Category: MG]] | ||
[[Category: gtp-binding]] | [[Category: gtp-binding]] | ||
[[Category: lipoprotein]] | [[Category: lipoprotein]] | ||
| Line 33: | Line 33: | ||
[[Category: transducer]] | [[Category: transducer]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 01:33:57 2008'' |
Revision as of 22:33, 30 March 2008
| |||||||
| , resolution 2.9Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , | ||||||
| Related: | 1ZCB
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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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