1zcb

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|RELATEDENTRY=[[1zca|1ZCA]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1zcb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1zcb OCA], [http://www.ebi.ac.uk/pdbsum/1zcb PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1zcb RCSB]</span>
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[[Category: Nance, M R.]]
[[Category: Nance, M R.]]
[[Category: Tesmer, J J.G.]]
[[Category: Tesmer, J J.G.]]
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[[Category: GDP]]
 
[[Category: gtp-binding]]
[[Category: gtp-binding]]
[[Category: lipoprotein]]
[[Category: lipoprotein]]
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[[Category: transducer]]
[[Category: transducer]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 23 14:27:48 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 01:33:53 2008''

Revision as of 22:34, 30 March 2008


PDB ID 1zcb

Drag the structure with the mouse to rotate
, resolution 2.00Å
Ligands:
Related: 1ZCA


Resources: FirstGlance, OCA, PDBsum, RCSB
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

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