Activating Compound | Comment | Organism | Structure |
---|---|---|---|
ATP | binding activates the enzyme complex to the R-state | Lactococcus lactis |
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 (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 | 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 | Comment | Organism | Structure |
---|---|---|---|
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 | Comment | Organism | Structure |
---|---|---|---|
Mg2+ | dependent on | Lactococcus lactis |
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 | UniProt | Comment | Textmining |
---|---|---|---|
Lactococcus lactis | - |
- |
- |
Purification (Comment) | Organism |
---|---|
recombinant wild-type and selenomethionine-labeled enzyme complex comprising subunits HisGs and HisZ from Escherichia coli | Lactococcus lactis |
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 |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + 5-phospho-alpha-D-ribose 1-diphosphate | - |
Lactococcus lactis | 1-(5-phospho-D-ribosyl)-ATP + diphosphate | - |
r | |
ATP + 5-phospho-alpha-D-ribose 1-diphosphate | first step in histidine biosynthesis | 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 | Comment | Organism |
---|---|---|
More | 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 | Comment | Organism |
---|---|---|
ATP phosphoribosyl transferase | - |
Lactococcus lactis |