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Literature summary for 4.3.3.7 extracted from

  • Reboul, C.F.; Porebski, B.T.; Griffin, M.D.; Dobson, R.C.; Perugini, M.A.; Gerrard, J.A.; Buckle, A.M.
    Structural and dynamic requirements for optimal activity of the essential bacterial enzyme dihydrodipicolinate synthase (2012), PLoS Comput. Biol., 8, e1002537.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 4.3.3.7

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-
Staphylococcus aureus
-
 a methicillin-resistant strain
-

Subunits

Subunits Comment Organism
dimer
-
 Staphylococcus aureus
More flexibility and its relationship to quaternary structure and function from molecular dynamic simulations of native tetrameric and mutant dimeric enzyme forms, it shows that the mutant dimeric enzyme form displays high flexibility, resulting in monomer reorientation within the dimer and increased flexibility at the tight-dimer interface, whereas the enzyme tetramer is relatively rigid. The enzyme dimer exhibits disorder within its active site with deformation of critical catalytic residues and removal of key hydrogen bonds that render it inactive Escherichia coli
More flexibility and its relationship to quaternary structure and function from molecular dynamic simulations show that the native dimeric enzyme form from a methicillin-resistant strain displays high flexibility, resulting in monomer reorientation within the dimer and increased flexibility at the tight-dimer interface and maintains its catalytic geometry and is thus fully functional Staphylococcus aureus
tetramer dimer of dimers Escherichia coli

Synonyms

Synonyms Comment Organism
DHDPS
-
 Staphylococcus aureus
DHDPS
-
 Escherichia coli
dihydrodipicolinate synthase
-
 Staphylococcus aureus
dihydrodipicolinate synthase
-
 Escherichia coli

General Information

General Information Comment Organism
additional information optimal activity is achieved by minimizing the inherent dimer flexibility using buttressing two dimers together in the case of the Escherichia coli tetrameric enzyme, active site structure simulations, overview Escherichia coli
additional information optimal activity is achieved by minimizing the inherent dimer flexibility using strengthening and extending the dimer interface in the dimeric Staphylococcus aurus MRSA strain enzyme, active site structure simulations, overview Staphylococcus aureus