2cfa
From Proteopedia
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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 [[1]], with EC number [2.1.1.148]. 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
Page seeded by OCA on Mon Oct 29 16:24:52 2007
Categories: Paramecium bursaria chlorella virus 1 | Protein complex | Bernauer, J. | Decottignies, P. | Graille, M. | Graziani, S. | Liebl, U. | Marchand, C. | Myllykallio, H. | Skouloubris, S. | Tilbeurgh, H.Van. | Zhou, C.Z. | CME | FAD | Fdts | Flavin dependent thymidylate synthase fad | Flavoprotein | Methyltransferase | Nucleotide biosynthesis | Paramecium bursaria chlorella virus-1 | Thyx | Transferase | Tscp
