Literature summary for 2.1.1.45 extracted from

Sapienza, P.J.; Popov, K.I.; Mowrey, D.D.; Falk, B.T.; Dokholyan, N.V.; Lee, A.L.
Inter-active site communication mediated by the dimer interface beta-sheet in the half-the-sites enzyme, thymidylate synthase (2019), Biochemistry, 58, 3302-3313 .

Crystallization (Commentary)

Crystallization (Comment)	Organism
determination of chemical shifts of the apoenzyme (lig0), the saturated holoenzyme (lig2), and the typically elusive singly bound (lig1) states. The two active sites in TS communicate with one another by using the intervening beta-sheet that also forms the dimer interface. The active sites have minimal communication in the lig0 state, but rather a network of correlated motions involving the two active sites is triggered by the first diligand binding event and amplified upon binding the second. Contacts between the diligand and a right-handed beta-bulge feature of this sheet are likely the triggering events	Escherichia coli

Crystallization (Comment)

Organism

determination of chemical shifts of the apoenzyme (lig0), the saturated holoenzyme (lig2), and the typically elusive singly bound (lig1) states. The two active sites in TS communicate with one another by using the intervening beta-sheet that also forms the dimer interface. The active sites have minimal communication in the lig0 state, but rather a network of correlated motions involving the two active sites is triggered by the first diligand binding event and amplified upon binding the second. Contacts between the diligand and a right-handed beta-bulge feature of this sheet are likely the triggering events

Escherichia coli

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	P0A884	-	-

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Release 2023.1 (January 2023)