2WBL
Three-dimensional structure of a binary ROP-PRONE complex
Summary for 2WBL
| Entry DOI | 10.2210/pdb2wbl/pdb |
| Descriptor | RHO OF PLANTS GUANINE NUCLEOTIDE EXCHANGE FACTOR 8, RAC-LIKE GTP-BINDING PROTEIN ARAC2 (2 entities in total) |
| Functional Keywords | membrane, prenylation, methylation, nucleotide- binding, signaling protein, nucleotide-binding, complex of prone-gef with rop substrate, lipoprotein, gtp-binding |
| Biological source | ARABIDOPSIS THALIANA (MOUSE-EAR CRESS) More |
| Cellular location | Cytoplasm (By similarity): Q38903 |
| Total number of polymer chains | 4 |
| Total formula weight | 122780.30 |
| Authors | Thomas, C.,Fricke, I.,Weyand, M.,Berken, A. (deposition date: 2009-03-02, release date: 2009-04-14, Last modification date: 2023-12-13) |
| Primary citation | Thomas, C.,Fricke, I.,Weyand, M.,Berken, A. 3D Structure of a Binary Rop-Prone Complex: The Final Intermediate for a Complete Set of Molecular Snapshots of the Ropgef Reaction. Biol.Chem., 390:427-, 2009 Cited by PubMed Abstract: Guanine nucleotide exchange factors (GEFs) catalyze the activation of GTP-binding proteins (G proteins) in a multi-step reaction comprising intermediary complexes with and without nucleotide. Rho proteins of plants (ROPs) are activated by novel RopGEFs with a catalytic PRONE domain. We have previously characterized structures of GDP-bound ROP and a ternary complex between plant-specific ROP nucleotide exchanger (PRONE) and ROP including loosely bound GDP. Now, we complete the molecular snapshots of the RopGEF reaction with the nucleotide-free ROP-PRONE structure at 2.9 A. The binary complex surprisingly closely resembles the preceding ternary intermediate including an unusually intact P-loop in the G protein. A striking difference is the prominent contact of the invariant P-loop lysine to a conserved switch II glutamate in ROP, favoring a key role of this interaction in driving out the nucleotide. The nucleotide-free state is supported by additional interactions involving the essential WW-motif in PRONE. We propose that this GEF region stabilizes the intact P-loop conformation, which facilitates re-association with a new nucleotide and further promotes the overall exchange reaction. With our novel structure, we provide further insights into the nucleotide exchange mechanism and present a first example of the complete GEF reaction at a molecular level. PubMed: 19335195DOI: 10.1515/BC.2009.049 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.9 Å) |
Structure validation
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