2CFA

Structure of viral flavin-dependant thymidylate synthase ThyX

2CFA の概要

• エントリーDOI: 10.2210/pdb2cfa/pdb
• 分子名称: THYMIDYLATE SYNTHASE, FLAVIN-ADENINE DINUCLEOTIDE, ... (4 entities in total)
• 機能のキーワード: fdts, tscp, flavin dependent thymidylate synthase fad, flavoprotein, nucleotide biosynthesis, methyltransferase, transferase
• 由来する生物種: PARAMECIUM BURSARIA CHLORELLA VIRUS 1; 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 51872.35

構造登録者

Graziani, S.,Bernauer, J.,Skouloubris, S.,Graille, M.,Zhou, C.-Z.,Marchand, C.,Decottignies, P.,van Tilbeurgh, H.,Myllykallio, H.,Liebl, U. (登録日: 2006-02-17, 公開日: 2006-05-16, 最終更新日: 2024-11-13)

主引用文献

Graziani, S.,Bernauer, J.,Skouloubris, S.,Graille, M.,Zhou, C.-Z.,Marchand, C.,Decottignies, P.,Van Tilbeurgh, H.,Myllykallio, H.,Liebl, U.
Catalytic Mechanism and Structure of Viral Flavin-Dependent Thymidylate Synthase Thyx.
J.Biol.Chem., 281:24048-, 2006

PubMed Abstract: By using biochemical and structural analyses, we have investigated the catalytic mechanism of the recently discovered flavin-dependent thymidylate synthase ThyX from Paramecium bursaria chlorella virus-1 (PBCV-1). Site-directed mutagenesis experiments have identified several residues implicated in either NADPH oxidation or deprotonation activity of PBCV-1 ThyX. Chemical modification by diethyl pyrocarbonate and mass spectroscopic analyses identified a histidine residue (His53) crucial for NADPH oxidation and located in the vicinity of the redox active N-5 atom of the FAD ring system. Moreover, we observed that the conformation of active site key residues of PBCV-1 ThyX differs from earlier reported ThyX structures, suggesting structural changes during catalysis. Steady-state kinetic analyses support a reaction mechanism where ThyX catalysis proceeds via formation of distinct ternary complexes without formation of a methyl enzyme intermediate.

PubMed: 16707489
DOI: 10.1074/JBC.M600745200

実験手法

X-RAY DIFFRACTION (2.3 Å)