Structural mechanism underlying the specific recognition between the arabidopsis state-transition phosphatase tap38/pph1 and phosphorylated light-harvesting complex protein lhcb1
文献类型：期刊论文
| 作者 | Wei, Xuepeng1,2; Guo, Jiangtao1; Li, Mei1; Liu, Zhenfeng1 |
| 刊名 | Plant cell
 |
| 出版日期 | 2015-04-01 |
| 卷号 | 27期号:4页码:1113-1127 |
| ISSN号 | 1040-4651 |
| DOI | 10.1105/tpc.15.00102 |
| 通讯作者 | Liu, zhenfeng(liuzf@sun5.ibp.ac.cn) |
| 英文摘要 | During state transitions, plants regulate energy distribution between photosystems i and ii through reversible phosphorylation and lateral migration of the major light-harvesting complex lhcii. dephosphorylation of lhcii and the transition from state 2 to state 1 requires a thylakoid membrane-associated phosphatase named tap38 or pph1. tap38/pph1 specifically targets lhcii but not the core subunits of photosystem ii, whereas the underlying molecular mechanism of their mutual recognition is currently unclear. here, we present the structures of arabidopsis thaliana tap38/pph1 in the substrate-free and substrate-bound states. the protein contains a type 2c serine/threonine protein phosphatase (pp2c) core domain, a mn2+ (or mg2+) binuclear center and two additional motifs contributing to substrate recognition. a 15-mer phosphorylated n-terminal peptide of lhcb1 binds to tap38/pph1 on two surface clefts enclosed by the additional motifs. the first segment of the phosphopeptide is clamped by a pair of tooth-like arginine residues at cleft 1 site. the binding adopts the lock-and-key mechanism with slight rearrangement of the substrate binding residues on tap38/pph1. meanwhile, a more evident substrate-induced fitting occurs on cleft 2 harboring the extended part of the phosphopeptide. the results unravel the bases for the specific recognition between tap38/pph1 and phosphorylated lhcb1, a crucial step in state transitions. |
| WOS关键词 | 3RD METAL-ION ; SERINE/THREONINE PHOSPHATASE ; PHOTOSYNTHETIC ACCLIMATION ; EXCITATION TRANSFER ; KINASES ; BINDING ; CHLOROPLASTS ; DEPHOSPHORYLATION ; CONFORMATION ; PLASTOQUINOL |
| WOS研究方向 | Biochemistry & Molecular Biology ; Plant Sciences ; Cell Biology |
| WOS类目 | Biochemistry & Molecular Biology ; Plant Sciences ; Cell Biology |
| 语种 | 英语 |
| WOS记录号 | WOS:000354822800015 |
| 出版者 | AMER SOC PLANT BIOLOGISTS |
| URI标识 | http://www.irgrid.ac.cn/handle/1471x/2376570 |
| 专题 | 中国科学院大学 |
| 通讯作者 | Liu, Zhenfeng |
| 作者单位 | 1.Chinese Acad Sci, Inst Biophys, Natl Lab Biomacromol, Beijing 100101, Peoples R China 2.Univ Chinese Acad Sci, Sch Life Sci, Beijing 100101, Peoples R China |
| 推荐引用方式 GB/T 7714 | Wei, Xuepeng,Guo, Jiangtao,Li, Mei,et al. Structural mechanism underlying the specific recognition between the arabidopsis state-transition phosphatase tap38/pph1 and phosphorylated light-harvesting complex protein lhcb1[J]. Plant cell,2015,27(4):1113-1127. |
| APA | Wei, Xuepeng,Guo, Jiangtao,Li, Mei,&Liu, Zhenfeng.(2015).Structural mechanism underlying the specific recognition between the arabidopsis state-transition phosphatase tap38/pph1 and phosphorylated light-harvesting complex protein lhcb1.Plant cell,27(4),1113-1127. |
| MLA | Wei, Xuepeng,et al."Structural mechanism underlying the specific recognition between the arabidopsis state-transition phosphatase tap38/pph1 and phosphorylated light-harvesting complex protein lhcb1".Plant cell 27.4(2015):1113-1127. |
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来源：中国科学院大学
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