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Crystal structure of Arabidopsis glutamyl-tRNA reductase in complex with its stimulator protein

文献类型：期刊论文

作者Zhao, Aiguo1; Fang, Ying1; Chen, Xuemin1; Zhao, Shun1; Dong, Wei1; Lin, Yajing2; Gong, Weimin2; Liu, Lin
刊名PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
出版日期2014
卷号111期号:18页码:6630-6635
ISSN号0027-8424
DOI10.1073/pnas.1400166111
文献子类Article
英文摘要Tetrapyrrole biosynthesis in plants, algae, and most bacteria starts from the NADPH-dependent reduction of glutamyl-tRNA by glutamyl- tRNA reductase (GluTR). The GluTR-catalyzed reaction is the rate-limiting step, and GluTR is the target of multiple posttranslational regulations, such as heme feedback inhibition, for the tetrapyrrole biosynthetic pathway. A recently identified GluTR regulator, GluTR binding protein (GluBP), has been shown to spatially organize tetrapyrrole synthesis by distributing GluTR into different suborganellar locations. Here we report the complex structure of GluTR-GluBP from Arabidopsis thaliana. The dimeric GluBP binds symmetrically to the catalytic domains of the V-shaped GluTR dimer via its C-terminal domain. A substantial conformational change of the GluTR NADPH-binding domain is observed, confirming the postulated rotation of the NADPH-binding domain for hydride transfer from NADPH to the substrate. Arg146, guarding the door for metabolic channeling, adopts alternative conformations, which may represent steps involved in substrate recognition and product release. A coupled enzyme assay shows that GluBP stimulates GluTR catalytic efficiency with an approximate threefold increase of the 5-aminolevulinic acid formation rate. In addition, the GluTR activity can be inhibited by heme in a concentration-dependent way regardless of the presence of GluBP. A structural alignment indicates that GluBP belongs to a heme-binding family involved in heme metabolism. We propose a catalytic mechanism model for GluTR, through which photosynthetic organisms can achieve precise regulation of tetrapyrrole biosynthesis.
学科主题Multidisciplinary Sciences
出版地WASHINGTON
电子版国际标准刊号1091-6490
WOS关键词TETRAPYRROLE BIOSYNTHESIS ; ESCHERICHIA-COLI ; 1ST ENZYME ; HEME ; RECOGNITION ; BINDING ; PLANTS ; FLU
WOS研究方向Science & Technology - Other Topics
语种英语
WOS记录号WOS:000335477300039
出版者NATL ACAD SCIENCES
资助机构National Natural Science Foundation of China [31370759] ; Ministry of Science and Technology of China [2011CBA00901] ; Hundred Talents Program of the Chinese Academy of Sciences
源URL[http://ir.ibcas.ac.cn/handle/2S10CLM1/27264]  
专题中科院光生物学重点实验室
作者单位1.Chinese Acad Sci, Inst Bot, Photosynth Res Ctr, Key Lab Photobiol, Beijing 100093, Peoples R China
2.Univ Chinese Acad Sci, Beijing 100049, Peoples R China
3.Chinese Acad Sci, Inst Biophys, Lab Noncoding RNA, Beijing 100101, Peoples R China
推荐引用方式
GB/T 7714		 Zhao, Aiguo,Fang, Ying,Chen, Xuemin,et al. Crystal structure of Arabidopsis glutamyl-tRNA reductase in complex with its stimulator protein[J]. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA,2014,111(18):6630-6635.
APA Zhao, Aiguo.,Fang, Ying.,Chen, Xuemin.,Zhao, Shun.,Dong, Wei.,...&Liu, Lin.(2014).Crystal structure of Arabidopsis glutamyl-tRNA reductase in complex with its stimulator protein.PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA,111(18),6630-6635.
MLA Zhao, Aiguo,et al."Crystal structure of Arabidopsis glutamyl-tRNA reductase in complex with its stimulator protein".PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA 111.18(2014):6630-6635.

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来源：植物研究所

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