7VS7
Crystal structure of the ectodomain of OsCERK1 in complex with chitin hexamer
7VS7 の概要
| エントリーDOI | 10.2210/pdb7vs7/pdb |
| 分子名称 | Chitin elicitor receptor kinase 1, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[alpha-L-fucopyranose-(1-3)][alpha-L-fucopyranose-(1-6)]2-acetamido-2-deoxy-beta-D-glucopyranose, ... (5 entities in total) |
| 機能のキーワード | cerk1, chitin, pamp, immunity, symbiosis, immune receptor, antifungal protein, transferase |
| 由来する生物種 | Oryza sativa Japonica Group (Japanese rice) |
| タンパク質・核酸の鎖数 | 1 |
| 化学式量合計 | 25918.27 |
| 構造登録者 | |
| 主引用文献 | Xu, L.,Wang, J.,Xiao, Y.,Han, Z.,Chai, J. Structural insight into chitin perception by chitin elicitor receptor kinase 1 of Oryza sativa. J Integr Plant Biol, 65:235-248, 2023 Cited by PubMed Abstract: Plants have developed innate immune systems to fight against pathogenic fungi by monitoring pathogenic signals known as pathogen-associated molecular patterns (PAMP) and have established endo symbiosis with arbuscular mycorrhizal (AM) fungi through recognition of mycorrhizal (Myc) factors. Chitin elicitor receptor kinase 1 of Oryza sativa subsp. Japonica (OsCERK1) plays a bifunctional role in mediating both chitin-triggered immunity and symbiotic relationships with AM fungi. However, it remains unclear whether OsCERK1 can directly recognize chitin molecules. In this study, we show that OsCERK1 binds to the chitin hexamer ((NAG) ) and tetramer ((NAG) ) directly and determine the crystal structure of the OsCERK1-(NAG) complex at 2 Å. The structure shows that one OsCERK1 is associated with one (NAG) . Upon recognition, chitin hexamer binds OsCERK1 by interacting with the shallow groove on the surface of LysM2. These structural findings, complemented by mutational analyses, demonstrate that LysM2 is crucial for recognition of both (NAG) and (NAG) . Altogether, these findings provide structural insights into the ability of OsCERK1 in chitin perception, which will lead to a better understanding of the role of OsCERK1 in mediating both immunity and symbiosis in rice. PubMed: 35568972DOI: 10.1111/jipb.13279 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.015 Å) |
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