Structural Basis of Reversible Phosphorylation by Maize Pyruvate Orthophosphate Dikinase Regulatory Protein

doi:10.1104/pp.15.01709

CORC > 植物研究所 > 中国科学院植物研究所 > 中科院光生物学重点实验室

	Structural Basis of Reversible Phosphorylation by Maize Pyruvate Orthophosphate Dikinase Regulatory Protein
	Jiang, Lun ; Chen, Yi-bo ; Zheng, Jiangge ; Chen, Zhenhang ; Liu, Yujie ; Tao, Ye 1; Wu, Wei ; Chen, Zhongzhou ; Wang, Bai-chen
刊名	PLANT PHYSIOLOGY
	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
电子版国际标准刊号	1532-2548
出版地	ROCKVILLE
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
出版者	AMER SOC PLANT BIOLOGISTS
WOS记录号	WOS:000369343300011
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]
内容类型	期刊论文
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.Chinese Acad Sci, Inst Bot, Key Lab Photobiol, Photosynth Res Ctr, Beijing 100093, Peoples R China 2.China Agr Univ, State Key Lab Agrobiotechnol, Beijing 100193, 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.