Crystallization (Comment) | Organism |
---|---|
crystal structures of pantothenate synthetase complexed with diphosphomethylphosphonic acid adenosyl ester and pantoate resolved at 1.6 A and of apo Escherichia coli pantothenate synthetase resolved at 1.70 A are used as the initial structures for the simulations | Escherichia coli |
crystal structures of pantothenate synthetase complexed with diphosphomethylphosphonic acid adenosyl ester and pantoate resolved at 1.6 A and of apo Escherichia coli pantothenate synthetase resolved at 1.70 A are used as the initial structures for the simulations | Mycobacterium tuberculosis |
Protein Variants | Comment | Organism |
---|---|---|
D63G | mutation increases the mobility of the gate loop in Escherichia coli pantothenate synthetase | Escherichia coli |
G74D | mutation reduces the mobility of the gate loop in Mycobacterium tuberculosis pantothenate synthetase | Mycobacterium tuberculosis |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | - |
- |
- |
Mycobacterium tuberculosis | - |
- |
- |
Subunits | Comment | Organism |
---|---|---|
dimer | molecular dynamics simulations show that the functional dynamics of the enzyme are dominated by motions of a flexible gate loop in the N-terminal domain and of the C-terminal domain. The gate loop motions dominate in Mycobacterium tuberculosis pantothenate synthetase while the C-terminal domain motion dominates in Escherichia coli pantothenate synthetase. Simulations also show that the correlated motions of the domains are severely compromised in the monomeric forms | Escherichia coli |
dimer | molecular dynamics simulations show that the functional dynamics of the enzyme are dominated by motions of a flexible gate loop in the N-terminal domain and of the C-terminal domain. The gate loop motions dominate in Mycobacterium tuberculosis pantothenate synthetase while the C-terminal domain motion dominates in Escherichia coli pantothenate synthetase. Simulations also show that the correlated motions of the domains are severely compromised in the monomeric forms | Mycobacterium tuberculosis |
Synonyms | Comment | Organism |
---|---|---|
Pantothenate synthetase | - |
Escherichia coli |
Pantothenate synthetase | - |
Mycobacterium tuberculosis |