2FTO

Y94F mutant of thymidylate synthase bound to thymidine-5'-phosphate and 10-propargyl-5,8-dideazafolid acid

Summary for 2FTO

• Entry DOI: 10.2210/pdb2fto/pdb
• Related: 2ftn 2ftq
• Descriptor: Thymidylate synthase, PHOSPHATE ION, THYMIDINE-5'-PHOSPHATE, ... (5 entities in total)
• Functional Keywords: methyltransferase, transferase
• Biological source: Escherichia coli
• Cellular location: Cytoplasm : P0A884
• Total number of polymer chains: 1
• Total formula weight: 31533.28

Authors

Roberts, S.A.,Montfort, W.R. (deposition date: 2006-01-24, release date: 2006-05-02, Last modification date: 2024-11-06)

Primary citation

Roberts, S.A.,Hyatt, D.C.,Honts, J.E.,Changchien, L.,Maley, G.F.,Maley, F.,Montfort, W.R.
Structure of the Y94F mutant of Escherichia coli thymidylate synthase.
ACTA CRYSTALLOGR.,SECT.F, 62:840-843, 2006

PubMed Abstract: Tyr94 of Escherichia coli thymidylate synthase is thought to be involved, either directly or by activation of a water molecule, in the abstraction of a proton from C5 of the 2'-deoxyuridine 5'-monophosphate (dUMP) substrate. Mutation of Tyr94 leads to a 400-fold loss in catalytic activity. The structure of the Y94F mutant has been determined in the native state and as a ternary complex with thymidine 5'-monophosphate (dTMP) and 10-propargyl 5,8-dideazafolate (PDDF). There are no structural changes ascribable to the mutation other than loss of a water molecule hydrogen bonded to the tyrosine OH, which is consistent with a catalytic role for the phenolic OH.

PubMed: 16946460
DOI: 10.1107/S1744309106029691

Experimental method

X-RAY DIFFRACTION (2 Å)