2NTY

Rop4-GDP-PRONE8

Summary for 2NTY

• Entry DOI: 10.2210/pdb2nty/pdb
• Related: 2NTX
• Descriptor: Emb|CAB41934.1, Rac-like GTP-binding protein ARAC5, GUANOSINE-5'-DIPHOSPHATE (3 entities in total)
• Functional Keywords: complex of prone-gef with rop substrate, signaling protein
• Biological source: Arabidopsis thaliana (thale cress); More
• Cellular location: Cytoplasm: Q38937
• Total number of polymer chains: 4
• Total formula weight: 123574.50

Authors

Thomas, C.,Fricke, I.,Scrima, A.,Berken, A.,Wittinghofer, A. (deposition date: 2006-11-08, release date: 2007-01-23, Last modification date: 2023-10-25)

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

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: 17218277
DOI: 10.1016/j.molcel.2006.11.023

Experimental method

X-RAY DIFFRACTION (3.1 Å)