期刊
SCIENCE
卷 335, 期 6064, 页码 85-88出版社
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/science.1215106
关键词
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资金
- Michigan Economic Development Corporation
- Office of Science of the U.S. Department of Energy
- Jay and Betty Van Andel Foundation
- Amway (China) Limited
- NIH
- NSF [IOS-0820508]
- Singapore Biomedical Research Council
- NUS Graduate School for Integrative Sciences and Engineering (NGS)
- National Institute for General Medical Studies [GM084041]
- Direct For Biological Sciences
- Division Of Integrative Organismal Systems [0820508] Funding Source: National Science Foundation
Abscisic acid (ABA) is an essential hormone for plants to survive environmental stresses. At the center of the ABA signaling network is a subfamily of type 2C protein phosphatases (PP2Cs), which form exclusive interactions with ABA receptors and subfamily 2 Snfl-related kinase (SnRK2s). Here, we report a SnRK2-PP2C complex structure, which reveals marked similarity in PP2C recognition by SnRK2 and ABA receptors. In the complex, the kinase activation loop docks into the active site of PP2C, while the conserved ABA-sensing tryptophan of PP2C inserts into the kinase catalytic cleft, thus mimicking receptor-PP2C interactions. These structural results provide a simple mechanism that directly couples ABA binding to SnRK2 kinase activation and highlight a new paradigm of kinase-phosphatase regulation through mutual packing of their catalytic sites.
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