Literature summary for 2.4.2.17 extracted from

Champagne, K.S.; Sissler, M.; Larrabee, Y.; Doublie, S.; Francklyn, C.S.
Activation of the hetero-octameric ATP phosphoribosyl transferase through subunit interface rearrangement by a tRNA synthetase paralog (2005), J. Biol. Chem., 280, 34096-34104.

Activating Compound

Activating Compound	Comment	Organism	Structure
ATP	binding activates the enzyme complex to the R-state	Lactococcus lactis

Cloned(Commentary)

Cloned (Comment)	Organism
overexpression of subunits HisGs and HisZ comprising complex in Escherichia coli strain BL21(DE3) as wild-type, or in strain B834 as selenomethionine-labeled complex	Lactococcus lactis

Crystallization (Commentary)

Crystallization (Comment)	Organism
purified recombinant wild-type and selenomethionine-labeled enzyme complex, the latter additionally by microseeding, hanging drop vapour diffusion method, 0.002 ml well solution containing 15-25% v/v PEG 400, 0.1 M Tris-HCl, pH 7.5, 0.2 M MgCl2, mixed with equal volume of protein solution containing 10-16 mg/ml protein, 10 mM ATP, or 10 mM N-1-methyl-ATP and 5 mM 5-phospho-alpha-D-ribose 1-diphosphate, crystal growth is dependent on ATP or N-1-methyl-ATP, derivatization with 2.5 mM sodium tungstate dihydrate, cryoprotection with 17-18% glycerol, X-ray diffraction structure determination and analysis at 2.9-3.2 A resolution	Lactococcus lactis

Crystallization (Comment)

Organism

purified recombinant wild-type and selenomethionine-labeled enzyme complex, the latter additionally by microseeding, hanging drop vapour diffusion method, 0.002 ml well solution containing 15-25% v/v PEG 400, 0.1 M Tris-HCl, pH 7.5, 0.2 M MgCl2, mixed with equal volume of protein solution containing 10-16 mg/ml protein, 10 mM ATP, or 10 mM N-1-methyl-ATP and 5 mM 5-phospho-alpha-D-ribose 1-diphosphate, crystal growth is dependent on ATP or N-1-methyl-ATP, derivatization with 2.5 mM sodium tungstate dihydrate, cryoprotection with 17-18% glycerol, X-ray diffraction structure determination and analysis at 2.9-3.2 A resolution

Lactococcus lactis

Protein Variants

Protein Variants	Comment	Organism
E130A	site-directed mutagenesis, about 60% reduced activity compared to the wild-type enzyme, no inhibition by histidine	Lactococcus lactis
Y268F/Y269F	site-directed mutagenesis, about 30% reduced activity compared to the wild-type enzyme, no inhibition by histidine	Lactococcus lactis

Inhibitors

Inhibitors	Comment	Organism
ADP	-	Lactococcus lactis
AMP	inhibits the enzyme complex together with histidine to the T-state	Lactococcus lactis
histidine	feedback inhibition, inhibits the enzyme complex together with ATP to the T-state, no inhibition of mutants E130A and Y268F/Y269F	Lactococcus lactis

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Mg2+	dependent on	Lactococcus lactis

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
ATP + 5-phospho-alpha-D-ribose 1-diphosphate	Lactococcus lactis	first step in histidine biosynthesis	1-(5-phospho-D-ribosyl)-ATP + diphosphate	-	r

Organism

Organism	UniProt	Comment	Textmining
Lactococcus lactis	-	-	-

Purification (Commentary)

Purification (Comment)	Organism
recombinant wild-type and selenomethionine-labeled enzyme complex comprising subunits HisGs and HisZ from Escherichia coli	Lactococcus lactis

Reaction

Reaction	Comment	Organism	Reaction ID
1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate = ATP + 5-phospho-alpha-D-ribose 1-diphosphate	substrate binding sites, active site structure, switch between active and inactive conformation	Lactococcus lactis	a

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.
ATP + 5-phospho-alpha-D-ribose 1-diphosphate	first step in histidine biosynthesis	Lactococcus lactis	1-(5-phospho-D-ribosyl)-ATP + diphosphate	-	r
ATP + 5-phospho-alpha-D-ribose 1-diphosphate	-	Lactococcus lactis	1-(5-phospho-D-ribosyl)-ATP + diphosphate	-	r
additional information	the enzyme comprises 4 catalytic subunits HisGs and 4 regulatory subunits HisZ with histidine as a ligand, 8 histidine binding sites at the subunit interfaces	Lactococcus lactis	?	-	?

Subunits

Subunits	Comment	Organism
additional information	overall structure and monomer architecture, several motif 2 loops in both subunit types, switch structure between active and inactive conformation	Lactococcus lactis
octamer	4 * catalytic subunit HisGs + 4 * regulatory subunit HisZ, (alpha,beta)4	Lactococcus lactis

Synonyms

Synonyms	Comment	Organism
ATP phosphoribosyl transferase	-	Lactococcus lactis