2cfa

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spinqualitylabelsall models 2cfa, resolution 2.30Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

STRUCTURE OF VIRAL FLAVIN-DEPENDANT THYMIDYLATE SYNTHASE THYX

Overview

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.

About this Structure

2CFA is a Protein complex structure of sequences from Paramecium bursaria chlorella virus 1 with CME and FAD as ligands. Active as Thymidylate synthase (FAD), with EC number 2.1.1.148 Known structural/functional Site: . Full crystallographic information is available from OCA.

Reference

Catalytic mechanism and structure of viral flavin-dependent thymidylate synthase ThyX., Graziani S, Bernauer J, Skouloubris S, Graille M, Zhou CZ, Marchand C, Decottignies P, van Tilbeurgh H, Myllykallio H, Liebl U, J Biol Chem. 2006 Aug 18;281(33):24048-57. Epub 2006 May 17. PMID:16707489

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