Literature summary for 1.2.1.70 extracted from

Zhang, M.; Zhang, F.; Fang, Y.; Chen, X.; Chen, Y.; Zhang, W.; Dai, H.E.; Lin, R.; Liu, L.
The non-canonical tetratricopeptide repeat (TPR) domain of fluorescent (FLU) mediates complex formation with glutamyl-tRNA reductase (2015), J. Biol. Chem., 290, 17559-17565 .

Cloned(Commentary)

Cloned (Comment)	Organism
gene HEMA1, recombinant co-overexpression of N-terminally His6-tagged FLUTPR and GluTRDD in Escherichia coli strain BL21(DE3)	Arabidopsis thaliana

Crystallization (Commentary)

Crystallization (Comment)	Organism
uncomplexed TPR domain of FLU (FLUTPR) and complex of the dimeric domain of GluTR bound to FLUTPR, hanging drop vapor diffusion method, from 0.2 M NaCl, 0.1 M Bis-Tris, pH 6.5, and 25% w/v PEG 3350 in 1 week, and from 0.15 M KBr and 30% w/v PEG monomethyl ether 2000, in 3 weeks, X-ray diffraction structure determination and analysis at 1.45 and 2.4 A resolution, respectively, molecular replacement and modeling	Arabidopsis thaliana

Crystallization (Comment)

Organism

uncomplexed TPR domain of FLU (FLUTPR) and complex of the dimeric domain of GluTR bound to FLUTPR, hanging drop vapor diffusion method, from 0.2 M NaCl, 0.1 M Bis-Tris, pH 6.5, and 25% w/v PEG 3350 in 1 week, and from 0.15 M KBr and 30% w/v PEG monomethyl ether 2000, in 3 weeks, X-ray diffraction structure determination and analysis at 1.45 and 2.4 A resolution, respectively, molecular replacement and modeling

Arabidopsis thaliana

Inhibitors

Inhibitors	Comment	Organism	Structure
protein FLU	the non-canonical tetratricopeptide repeat (TPR) domain of fluorescent (FLU) mediates complex formation with glutamyl-tRNA reductase. Protein FLU negatively regulates glutamyl-tRNA reductase (GluTR) during chlorophyll biosynthesis. A 2:2 FLUTPR-GluTR complex is the functional unit for FLU-mediated GluTR regulation. Enzyme binding complex structure analysis from crystal structures, detailed overview	Arabidopsis thaliana

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
L-glutamate 1-semialdehyde + NADP+ + tRNAGlu	Arabidopsis thaliana	-	L-glutamyl-tRNAGlu + NADPH + H+	-	?

Organism

Organism	UniProt	Comment	Textmining
Arabidopsis thaliana	P42804	-	-

Purification (Commentary)

Purification (Comment)	Organism
recombinant N-terminally His6-tagged FLUTPR and GluTRDD in Escherichia coli strain BL21(DE3)	Arabidopsis thaliana

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
L-glutamate 1-semialdehyde + NADP+ + tRNAGlu	-	Arabidopsis thaliana	L-glutamyl-tRNAGlu + NADPH + H+	-	?

Synonyms

Synonyms	Comment	Organism
GluTR	-	Arabidopsis thaliana
HEMA1	-	Arabidopsis thaliana

Cofactor

Cofactor	Comment	Organism	Structure
NADP+	-	Arabidopsis thaliana

General Information

General Information	Comment	Organism
physiological function	protein FLU negatively regulates glutamyl-tRNA reductase (GluTR) during chlorophyll biosynthesis. It directly interacts through its TPR domain with glutamyl-tRNA reductase (GluTR), the rate-limiting enzyme in the formation of 5-aminolevulinic acid. The formation of the FLU-GluTR complex prevents glutamyl-tRNA, the GluTR substrate, from binding with this enzyme	Arabidopsis thaliana