2cfa

From Proteopedia

Revision as of 15:01, 30 October 2007

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, ... [(full description)]

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]. Structure known Active Site: AC1. 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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