期刊
JOURNAL OF BIOLOGICAL CHEMISTRY
卷 288, 期 50, 页码 35868-35876出版社
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
DOI: 10.1074/jbc.M113.517417
关键词
Plant Molecular Biology; Protein Structure; Protein; Protein Interactions; Structural Biology; X-ray Crystallography; RanGAP; Rx; Coiled-coil Domain; Plant Resistance Protein
资金
- National Outstanding Young Scholar Science Foundation of China Grant [20101331722]
- National Science Foundation Grant [IOB-0343327]
- National Science Foundation graduate research fellowship
Background: The interaction of the potato disease resistance protein Rx with RanGAP2 is important for virus resistance. Results: The crystal structure of the complex of the Rx and RanGAP2 N-terminal domains was determined. Conclusion: The two proteins bind primarily through hydrophobic interactions. Significance: This work reveals the distinct surfaces of the Rx coiled-coil domain involved in intra- and intermolecular interactions. 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.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据