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

doi:10.1073/pnas.1400166111

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	Crystal structure of Arabidopsis glutamyl-tRNA reductase in complex with its stimulator protein
	Zhao, Aiguo 1; Fang, Ying 1; Chen, Xuemin 1; Zhao, Shun 1; Dong, Wei 1; Lin, Yajing 2; Gong, Weimin 2; Liu, Lin
	2014
发表期刊	PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
ISSN	0027-8424
卷号	111 期号:18 页码:6630-6635
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.
学科领域	Multidisciplinary Sciences
DOI	10.1073/pnas.1400166111
收录类别	SCI
语种	英语
WOS关键词	TETRAPYRROLE BIOSYNTHESIS ; ESCHERICHIA-COLI ; 1ST ENZYME ; HEME ; RECOGNITION ; BINDING ; PLANTS ; FLU
WOS研究方向	Science & Technology - Other Topics
WOS记录号	WOS:000335477300039
出版者	NATL ACAD SCIENCES
文献子类	Article
出版地	WASHINGTON
EISSN	1091-6490
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
作者邮箱	liulin@ibcas.ac.cn
作品OA属性	Green Published
引用统计	被引频次：48[WOS] [WOS记录] [WOS相关记录]
文献类型	期刊论文
条目标识符	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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