Structural Basis of Reversible Phosphorylation by Maize Pyruvate Orthophosphate Dikinase Regulatory Protein
文献类型：期刊论文
| 作者 | Jiang, Lun; Chen, Yi-bo; Zheng, Jiangge; Chen, Zhenhang; Liu, Yujie; Tao, Ye2; Wu, Wei; Chen, Zhongzhou; Wang, Bai-chen |
| 刊名 | PLANT PHYSIOLOGY
 |
| 出版日期 | 2016 |
| 卷号 | 170期号:2页码:732-741 |
| ISSN号 | 0032-0889 |
| DOI | 10.1104/pp.15.01709 |
| 文献子类 | Article |
| 英文摘要 | Pyruvate orthophosphate dikinase (PPDK) is one of the most important enzymes in C-4 photosynthesis. PPDK regulatory protein (PDRP) regulates the inorganic phosphate-dependent activation and ADP-dependent inactivation of PPDK by reversible phosphorylation. PDRP shares no significant sequence similarity with other protein kinases or phosphatases. To investigate the molecular mechanism by which PDRP carries out its dual and competing activities, we determined the crystal structure of PDRP from maize (Zea mays). PDRP forms a compact homo-dimer in which each protomer contains two separate N-terminal (NTD) and C-terminal (CTD) domains. The CTD includes several key elements for performing both phosphorylation and dephosphorylation activities: the phosphate binding loop (P-loop) for binding the ADP and inorganic phosphate substrates, residues Lys-274 and Lys-299 for neutralizing the negative charge, and residue Asp-277 for protonating and deprotonating the target Thr residue of PPDK to promote nucleophilic attack. Surprisingly, the NTD shares the same protein fold as the CTD and also includes a putative P-loop with AMP bound but lacking enzymatic activities. Structural analysis indicated that this loop may participate in the interaction with and regulation of PPDK. The NTD has conserved intramolecular and intermolecular disulfide bonds for PDRP dimerization. Moreover, PDRP is the first structure of the domain of unknown function 299 enzyme family reported. This study provides a structural basis for understanding the catalytic mechanism of PDRP and offers a foundation for the development of selective activators or inhibitors that may regulate photosynthesis. |
| 学科主题 | Plant Sciences |
| 出版地 | ROCKVILLE |
| 电子版国际标准刊号 | 1532-2548 |
| WOS关键词 | X-RAY STRUCTURE ; C-4 PHOTOSYNTHESIS ; CRYSTAL-STRUCTURE ; HPR-KINASE/PHOSPHATASE ; BIFUNCTIONAL PROTEIN ; SHIKIMATE KINASE ; PI DIKINASE ; ACTIVATION ; INACTIVATION ; MECHANISM |
| WOS研究方向 | Science Citation Index Expanded (SCI-EXPANDED) |
| 语种 | 英语 |
| WOS记录号 | WOS:000369343300011 |
| 出版者 | AMER SOC PLANT BIOLOGISTS |
| 资助机构 | State Key Program of National Natural Science of ChinaNational Natural Science Foundation of China (NSFC) [31030017] ; National Natural Science Foundation of ChinaNational Natural Science Foundation of China (NSFC) [31222032, 31370720] ; Extramural Scientists of State Key Laboratory of Agrobiotechnology [2016SKLAB6-1] |
| 源URL | [http://ir.ibcas.ac.cn/handle/2S10CLM1/25324]  |
| 专题 | 中科院光生物学重点实验室 |
| 作者单位 | 1.China Agr Univ, State Key Lab Agrobiotechnol, Beijing 100193, Peoples R China 2.Chinese Acad Sci, Inst Bot, Key Lab Photobiol, Photosynth Res Ctr, Beijing 100093, Peoples R China 3.Chinese Acad Sci, Inst High Energy Phys, Beijing Synchrotron Radiat Facil, Beijing 100049, Peoples R China |
| 推荐引用方式 GB/T 7714 | Jiang, Lun,Chen, Yi-bo,Zheng, Jiangge,et al. Structural Basis of Reversible Phosphorylation by Maize Pyruvate Orthophosphate Dikinase Regulatory Protein[J]. PLANT PHYSIOLOGY,2016,170(2):732-741. |
| APA | Jiang, Lun.,Chen, Yi-bo.,Zheng, Jiangge.,Chen, Zhenhang.,Liu, Yujie.,...&Wang, Bai-chen.(2016).Structural Basis of Reversible Phosphorylation by Maize Pyruvate Orthophosphate Dikinase Regulatory Protein.PLANT PHYSIOLOGY,170(2),732-741. |
| MLA | Jiang, Lun,et al."Structural Basis of Reversible Phosphorylation by Maize Pyruvate Orthophosphate Dikinase Regulatory Protein".PLANT PHYSIOLOGY 170.2(2016):732-741. |
入库方式： OAI收割
来源：植物研究所
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