1CC0
CRYSTAL STRUCTURE OF THE RHOA.GDP-RHOGDI COMPLEX
Summary for 1CC0
| Entry DOI | 10.2210/pdb1cc0/pdb |
| Descriptor | transforming protein rhoA, rho GDP dissociation inhibitor alpha, MAGNESIUM ION, ... (4 entities in total) |
| Functional Keywords | rho gtpase, g-protein, signaling protein |
| Biological source | Homo sapiens (human) More |
| Total number of polymer chains | 4 |
| Total formula weight | 90292.48 |
| Authors | Longenecker, K.L.,Read, P.,Derewenda, U.,Dauter, Z.,Garrard, S.,Walker, L.,Somlyo, A.V.,Somlyo, A.P.,Nakamoto, R.K.,Derewenda, Z.S. (deposition date: 1999-03-03, release date: 2000-01-07, Last modification date: 2023-12-27) |
| Primary citation | Longenecker, K.,Read, P.,Derewenda, U.,Dauter, Z.,Liu, X.,Garrard, S.,Walker, L.,Somlyo, A.V.,Nakamoto, R.K.,Somlyo, A.P.,Derewenda, Z.S. How RhoGDI binds Rho. Acta Crystallogr.,Sect.D, 55:1503-1515, 1999 Cited by PubMed Abstract: Like all Rho (Ras homology) GTPases, RhoA functions as a molecular switch in cell signaling, alternating between GTP- and GDP-bound states, with its biologically inactive GDP-bound form maintained as a cytosolic complex with RhoGDI (guanine nucleotide-exchange inhibitor). The crystal structures of RhoA-GDP and of the C-terminal immunoglobulin-like domain of RhoGDI (residues 67-203) are known, but the mechanism by which the two proteins interact is not known. The functional human RhoA-RhoGDI complex has been expressed in yeast and crystallized (P6(5)22, unit-cell parameters a = b = 139, c = 253 A, two complexes in the asymmetric unit). Although diffraction from these crystals extends to 3.5 A and is highly anisotropic, the experimentally phased (MAD plus MIR) electron-density map was adequate to reveal the mutual disposition of the two molecules. The result was validated by molecular-replacement calculations when data were corrected for anisotropy. Furthermore, the N-terminus of RhoGDI (the region involved in inhibition of nucleotide exchange) can be identified in the electron-density map: it is bound to the switch I and switch II regions of RhoA, occluding an epitope which binds Dbl-like nucleotide-exchange factors. The entrance of the hydrophobic pocket of RhoGDI is 25 A from the last residue in the RhoA model, with its C-terminus oriented to accommodate the geranylgeranyl group without conformational change in RhoA. PubMed: 10489445DOI: 10.1107/S090744499900801X PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (5 Å) |
Structure validation
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