Literature summary for 1.5.1.3 extracted from

Oyen, D.; Fenwick, R.B.; Aoto, P.C.; Stanfield, R.L.; Wilson, I.A.; Dyson, H.J.; Wright, P.E.
Defining the structural basis for allosteric product release from E. coli dihydrofolate reductase using NMR relaxation dispersion (2017), J. Am. Chem. Soc., 139, 11233-11240 .

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Crystallization (Commentary)

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

Protein Variants	Comment	Organism
L28F	mutant behaves similarly to wild-type	Escherichia coli

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	P0ABQ4	-	-

Synonyms

Synonyms	Comment	Organism
folA	-	Escherichia coli

Cofactor

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

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Release 2023.1 (January 2023)