1a2b
From Proteopedia
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|PDB= 1a2b |SIZE=350|CAPTION= <scene name='initialview01'>1a2b</scene>, resolution 2.4Å | |PDB= 1a2b |SIZE=350|CAPTION= <scene name='initialview01'>1a2b</scene>, resolution 2.4Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=GSP:5'-GUANOSINE-DIPHOSPHATE-MONOTHIOPHOSPHATE'>GSP</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=1a2b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1a2b OCA], [http://www.ebi.ac.uk/pdbsum/1a2b PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1a2b RCSB]</span> | ||
}} | }} | ||
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[[Category: Shimizu, T.]] | [[Category: Shimizu, T.]] | ||
[[Category: Shirakawa, M.]] | [[Category: Shirakawa, M.]] | ||
| - | [[Category: GSP]] | ||
| - | [[Category: MG]] | ||
[[Category: gtpase]] | [[Category: gtpase]] | ||
[[Category: oncogene protein]] | [[Category: oncogene protein]] | ||
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[[Category: small g-protein]] | [[Category: small g-protein]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 18:31:31 2008'' |
Revision as of 15:31, 30 March 2008
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| , resolution 2.4Å | |||||||
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| Ligands: | , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
HUMAN RHOA COMPLEXED WITH GTP ANALOGUE
Overview
The 2.4-A resolution crystal structure of a dominantly active form of the small guanosine triphosphatase (GTPase) RhoA, RhoAV14, complexed with the nonhydrolyzable GTP analogue, guanosine 5'-3-O-(thio)triphosphate (GTPgammaS), reveals a fold similar to RhoA-GDP, which has been recently reported (Wei, Y., Zhang, Y., Derewenda, U., Liu, X., Minor, W., Nakamoto, R. K., Somlyo, A. V., Somlyo, A. P., and Derewenda, Z. S. (1997) Nat. Struct. Biol. 4, 699-703), but shows large conformational differences localized in switch I and switch II. These changes produce hydrophobic patches on the molecular surface of switch I, which has been suggested to be involved in its effector binding. Compared with H-Ras and other GTPases bound to GTP or GTP analogues, the significant conformational differences are located in regions involving switches I and II and part of the antiparallel beta-sheet between switches I and II. Key residues that produce these conformational differences were identified. In addition to these differences, RhoA contains four insertion or deletion sites with an extra helical subdomain that seems to be characteristic of members of the Rho family, including Rac1, but with several variations in details. These sites also display large displacements from those of H-Ras. The ADP-ribosylation residue, Asn41, by C3-like exoenzymes stacks on the indole ring of Trp58 with a hydrogen bond to the main chain of Glu40. The recognition of the guanosine moiety of GTPgammaS by the GTPase contains water-mediated hydrogen bonds, which seem to be common in the Rho family. These structural differences provide an insight into specific interaction sites with the effectors, as well as with modulators such as guanine nucleotide exchange factor (GEF) and guanine nucleotide dissociation inhibitor (GDI).
About this Structure
1A2B is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Crystal structure of human RhoA in a dominantly active form complexed with a GTP analogue., Ihara K, Muraguchi S, Kato M, Shimizu T, Shirakawa M, Kuroda S, Kaibuchi K, Hakoshima T, J Biol Chem. 1998 Apr 17;273(16):9656-66. PMID:9545299
Page seeded by OCA on Sun Mar 30 18:31:31 2008
