1tx4
From Proteopedia
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|PDB= 1tx4 |SIZE=350|CAPTION= <scene name='initialview01'>1tx4</scene>, resolution 1.65Å | |PDB= 1tx4 |SIZE=350|CAPTION= <scene name='initialview01'>1tx4</scene>, resolution 1.65Å | ||
|SITE= <scene name='pdbsite=TS:Transition+State+Analog+Gdp.Alf4'>TS</scene> | |SITE= <scene name='pdbsite=TS:Transition+State+Analog+Gdp.Alf4'>TS</scene> | ||
| - | |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= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1tx4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tx4 OCA], [http://www.ebi.ac.uk/pdbsum/1tx4 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1tx4 RCSB]</span> | ||
}} | }} | ||
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[[Category: Smerdon, S J.]] | [[Category: Smerdon, S J.]] | ||
[[Category: Walker, P A.]] | [[Category: Walker, P A.]] | ||
| - | [[Category: ALF]] | ||
| - | [[Category: GDP]] | ||
| - | [[Category: MG]] | ||
[[Category: complex (gtpase activation/proto-oncogene)]] | [[Category: complex (gtpase activation/proto-oncogene)]] | ||
[[Category: gap]] | [[Category: gap]] | ||
| Line 34: | Line 34: | ||
[[Category: transition state]] | [[Category: transition state]] | ||
| - | ''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 00:02:19 2008'' |
Revision as of 21:02, 30 March 2008
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| , resolution 1.65Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | |||||||
| Ligands: | , , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
RHO/RHOGAP/GDP(DOT)ALF4 COMPLEX
Overview
Small G proteins of the Rho family, which includes Rho, Rac and Cdc42Hs, regulate phosphorylation pathways that control a range of biological functions including cytoskeleton formation and cell proliferation. They operate as molecular switches, cycling between the biologically active GTP-bound form and the inactive GDP-bound state. Their rate of hydrolysis of GTP to GDP by virtue of their intrinsic GTPase activity is slow, but can be accelerated by up to 10(5)-fold through interaction with rhoGAP, a GTPase-activating protein that stimulates Rho-family proteins. As such, rhoGAP plays a crucial role in regulating Rho-mediated signalling pathways. Here we report the crystal structure of RhoA and rhoGAP complexed with the transition-state analogue GDP.AlF4- at 1.65 A resolution. There is a rotation of 20 degrees between the Rho and rhoGAP proteins in this complex when compared with the ground-state complex Cdc42Hs.GMPPNP/rhoGAP, in which Cdc42Hs is bound to the non-hydrolysable GTP analogue GMPPNP. Consequently, in the transition state complex but not in the ground state, the rhoGAP domain contributes a residue, Arg85(GAP) directly into the active site of the G protein. We propose that this residue acts to stabilize the transition state of the GTPase reaction. RhoGAP also appears to function by stabilizing several regions of RhoA that are important in signalling the hydrolysis of GTP.
About this Structure
1TX4 is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Structure at 1.65 A of RhoA and its GTPase-activating protein in complex with a transition-state analogue., Rittinger K, Walker PA, Eccleston JF, Smerdon SJ, Gamblin SJ, Nature. 1997 Oct 16;389(6652):758-62. PMID:9338791
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