Literature summary for 2.5.1.54 extracted from

Cui, D.; Deng, A.; Bai, H.; Yang, Z.; Liang, Y.; Liu, Z.; Qiu, Q.; Wang, L.; Liu, S.; Zhang, Y.; Shi, Y.; Qi, J.; Wen, T.
Molecular basis for feedback inhibition of tyrosine-regulated 3-deoxy-D-arabino-heptulosonate-7-phosphate synthase from Escherichia coli (2019), J. Struct. Biol., 206, 322-334 .

Crystallization (Commentary)

Crystallization (Comment)	Organism
structures of apo form and complex with the inhibitor tyrosine at 2.5 and 2.0 A resolutions, respectively. DAHPS(Tyr) has a typical (beta/alpha)8 TIM barrel, which is decorated with an N-terminal extension and an antiparallel beta sheet. Inhibitor tyrosine binds at a cavity formed by residues of helices alpha3, alpha4, strands beta6a, beta6b and the adjacent loops, and directly interacts with residues P148, Q152, S181, I213 and N8*. Conformational changes of residues P148, Q152 and I213 initiate a transmission pathway to propagate the allosteric signal from the tyrosine-binding site to the active site	Escherichia coli

Crystallization (Comment)

Organism

structures of apo form and complex with the inhibitor tyrosine at 2.5 and 2.0 A resolutions, respectively. DAHPS(Tyr) has a typical (beta/alpha)8 TIM barrel, which is decorated with an N-terminal extension and an antiparallel beta sheet. Inhibitor tyrosine binds at a cavity formed by residues of helices alpha3, alpha4, strands beta6a, beta6b and the adjacent loops, and directly interacts with residues P148, Q152, S181, I213 and N8*. Conformational changes of residues P148, Q152 and I213 initiate a transmission pathway to propagate the allosteric signal from the tyrosine-binding site to the active site

Escherichia coli

Protein Variants

Protein Variants	Comment	Organism
I213P	overexpression of variant leads to less decrease in the accumulation of phenylalanine than overexpression of wild-type	Escherichia coli
N8A	overexpression of variant leads to less decrease in the accumulation of phenylalanine than overexpression of wild-type	Escherichia coli
P148A	overexpression of variant leads to less decrease in the accumulation of phenylalanine than overexpression of wild-type	Escherichia coli
Q152A	overexpression of variant leads to higher accumulation of phenylalanine	Escherichia coli
S181A	overexpression of variant leads to higher accumulation of phenylalanine	Escherichia coli

Inhibitors

Inhibitors	Comment	Organism	Structure
L-tyrosine	-	Escherichia coli

Molecular Weight [Da]

Molecular Weight [Da]	Molecular Weight Maximum [Da]	Comment	Organism
77000	-	sedimentation velocity data, apo protein	Escherichia coli
78000	-	sedimentation velocity data, in complex with tyrosine	Escherichia coli

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	P00888	isoform is Tyr-sensitive	-
Escherichia coli K12	P00888	isoform is Tyr-sensitive	-

Subunits

Subunits	Comment	Organism
dimer	2 * 38800, calculated from sequence	Escherichia coli

Synonyms

Synonyms	Comment	Organism
DAHPS(Tyr)	-	Escherichia coli