Application | Comment | Organism |
---|---|---|
additional information | the catalytic site at the alphaTP-betaTP interface is loaded first upon addition of nucleotides to nucleotide-depleted F1-ATPases | Escherichia coli |
Cloned (Comment) | Organism |
---|---|
mutant plasmids expressed in Escherichia coli strain JM103 | Escherichia coli |
Crystallization (Comment) | Organism |
---|---|
catalytic site at the alphaTP-betaTP interface with bound MgADP- in crystal structures represents a catalytic site containing inhibitory MgADP- | Escherichia coli |
Protein Variants | Comment | Organism |
---|---|---|
additional information | (alpha V371C)3(beta R337C)3 gamma double mutant, steady state ATPase activity is 30% of that of the wild-type | Escherichia coli |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
AlCl3 | irreversibly inactivates the steady state ATPase activity of the reduced double mutant or the cross-linked enzyme after incubation of stoichiometric or 0.2 mM MgADP- | Escherichia coli | |
MgADP- | irreversibly inactivates the steady state ATPase activity of the reduced double mutant or the cross-linked enzyme after addition of AlCl3 and NaF | Escherichia coli | |
NaF | irreversibly inactivates the steady state ATPase activity of the reduced double mutant or the cross-linked enzyme after incubation of stoichiometric or 0.2 mM MgADP- | Escherichia coli |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | - |
- |
- |
Synonyms | Comment | Organism |
---|---|---|
TF1-ATPase | - |
Escherichia coli |