2FTO

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

2FTO の概要

• エントリーDOI: 10.2210/pdb2fto/pdb
• 関連するPDBエントリー: 2ftn 2ftq
• 分子名称: Thymidylate synthase, PHOSPHATE ION, THYMIDINE-5'-PHOSPHATE, ... (5 entities in total)
• 機能のキーワード: methyltransferase, transferase
• 由来する生物種: Escherichia coli
• 細胞内の位置: Cytoplasm : P0A884
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 31533.28

構造登録者

Roberts, S.A.,Montfort, W.R. (登録日: 2006-01-24, 公開日: 2006-05-02, 最終更新日: 2024-11-06)

主引用文献

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

実験手法

X-RAY DIFFRACTION (2 Å)