2cfa | pdb_00002cfa
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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
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Proteopedia Page Contributors and Editors (what is this?)
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- 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
