4M70

Crystal structure of potato Rx-CC domain in complex with RanGAP2-WPP domain

Summary for 4M70

• Entry DOI: 10.2210/pdb4m70/pdb
• Descriptor: Rx protein, Ran GTPase activating protein 2, ... (4 entities in total)
• Functional Keywords: rx, rangap2, coiled coil domain, wpp domain, plant disease resistance gene, resistance responses, popato x virus, plant protein
• Biological source: Solanum tuberosum (potato); More
• Total number of polymer chains: 10
• Total formula weight: 125938.79

Authors

Chai, J.,Hao, W. (deposition date: 2013-08-12, release date: 2013-11-13, Last modification date: 2024-03-20)

Primary citation

Hao, W.,Collier, S.M.,Moffett, P.,Chai, J.
Structural Basis for the Interaction between the Potato Virus X Resistance Protein (Rx) and Its Cofactor Ran GTPase-activating Protein 2 (RanGAP2)
J.Biol.Chem., 288:35868-35876, 2013

PubMed Abstract: The potato (Solanum tuberosum) disease resistance protein Rx has a modular arrangement that contains coiled-coil (CC), nucleotide-binding (NB), and leucine-rich repeat (LRR) domains and mediates resistance to potato virus X. The Rx N-terminal CC domain undergoes an intramolecular interaction with the Rx NB-LRR region and an intermolecular interaction with the Rx cofactor RanGAP2 (Ran GTPase-activating protein 2). Here, we report the crystal structure of the Rx CC domain in complex with the Trp-Pro-Pro (WPP) domain of RanGAP2. The structure reveals that the Rx CC domain forms a heterodimer with RanGAP2, in striking contrast to the homodimeric structure of the CC domain of the barley disease resistance protein MLA10. Structure-based mutagenesis identified residues from both the Rx CC domain and the RanGAP2 WPP domain that are crucial for their interaction and function in vitro and in vivo. Our results reveal the molecular mechanism underlying the interaction of Rx with RanGAP2 and identify the distinct surfaces of the Rx CC domain that are involved in intramolecular and intermolecular interactions.

PubMed: 24194517
DOI: 10.1074/jbc.M113.517417

Experimental method

X-RAY DIFFRACTION (2.103 Å)