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Literature summary extracted from

  • Tan, Y.S.; Fuentes, G.; Verma, C.
    A comparison of the dynamics of pantothenate synthetase from M. tuberculosis and E. coli: computational studies (2011), Proteins, 79, 1715-1727.
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
6.3.2.1 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
6.3.2.1 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

EC Number Protein Variants Comment Organism
6.3.2.1 D63G mutation increases the mobility of the gate loop in Escherichia coli pantothenate synthetase Escherichia coli
6.3.2.1 G74D mutation reduces the mobility of the gate loop in Mycobacterium tuberculosis pantothenate synthetase Mycobacterium tuberculosis

Organism

EC Number Organism UniProt Comment Textmining
6.3.2.1 Escherichia coli
-
-
-
6.3.2.1 Mycobacterium tuberculosis
-
-
-

Subunits

EC Number Subunits Comment Organism
6.3.2.1 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
6.3.2.1 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

EC Number Synonyms Comment Organism
6.3.2.1 Pantothenate synthetase
-
 Escherichia coli
6.3.2.1 Pantothenate synthetase
-
 Mycobacterium tuberculosis