2NTX
Prone8
Summary for 2NTX
| Entry DOI | 10.2210/pdb2ntx/pdb |
| Related | 2NTY |
| Descriptor | Emb|CAB41934.1 (2 entities in total) |
| Functional Keywords | dimer, guanine nucleotide exchange factor, signaling protein |
| Biological source | Arabidopsis thaliana (thale cress) |
| Total number of polymer chains | 2 |
| Total formula weight | 84345.79 |
| Authors | Thomas, C.,Fricke, I.,Scrima, A.,Berken, A.,Wittinghofer, A. (deposition date: 2006-11-08, release date: 2007-01-23, Last modification date: 2024-11-13) |
| Primary citation | Thomas, C.,Fricke, I.,Scrima, A.,Berken, A.,Wittinghofer, A. Structural Evidence for a Common Intermediate in Small G Protein-GEF Reactions Mol.Cell, 25:141-149, 2007 Cited by PubMed Abstract: Rho of plants (Rop) proteins belong to the superfamily of small GTP-binding (G) proteins and are vital regulators of signal transduction in plants. In order to become activated, Rop proteins need to exchange GDP for GTP, an intrinsically slow process catalyzed by guanine nucleotide exchange factors (GEFs). RopGEFs show no homology to animal RhoGEFs, and the catalytic mechanism remains elusive. GEF-catalysed nucleotide exchange proceeds via transient ternary and stable binary complexes. While a number of structural studies have analyzed binary nucleotide-free G protein-GEF complexes, very little is known about the ternary complexes. Here we report the X-ray structure of the catalytic PRONE domain of RopGEF8 from Arabidopsis thaliana, both alone and in a ternary complex with Rop4 and GDP. The features of the latter complex, a transient intermediate of the exchange reaction never directly observed before, suggest a common mechanism of catalyzed nucleotide exchange applicable to small G proteins in general. PubMed: 17218277DOI: 10.1016/j.molcel.2006.11.023 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.2 Å) |
Structure validation
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