Crystallization (Comment) | Organism |
---|---|
in the excited state of the enzyme:THF:NADPH product release complex, the reduced nicotinamide ring of the cofactor transiently enters the active site where it displaces the pterin ring of the THF product. The p-aminobenzoyl-L-glutamate tail of THF remains weakly bound in a widened binding cleft | Escherichia coli |
Protein Variants | Comment | Organism |
---|---|---|
L28F | mutant behaves similarly to wild-type | Escherichia coli |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | P0ABQ4 | - |
- |
Synonyms | Comment | Organism |
---|---|---|
folA | - |
Escherichia coli |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
NADPH | transient entry of the reduced nicotinamide moiety into the active site pocket causes a steric clash with the pterin ring of the product tetrahydrofolate, facilitating release of the pterin ring from the active site. Transient binding of the ribose moiety causes helix C to shift, thereby opening the pABG cleft and further assisting product release | Escherichia coli |