This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
2cfa
From Proteopedia
| Line 4: | Line 4: | ||
==Overview== | ==Overview== | ||
| - | By using biochemical and structural analyses, we have investigated the | + | 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== | ==About this Structure== | ||
| Line 22: | Line 22: | ||
[[Category: Myllykallio, H.]] | [[Category: Myllykallio, H.]] | ||
[[Category: Skouloubris, S.]] | [[Category: Skouloubris, S.]] | ||
| - | [[Category: Tilbeurgh, H | + | [[Category: Tilbeurgh, H Van.]] |
| - | [[Category: Zhou, C | + | [[Category: Zhou, C Z.]] |
[[Category: CME]] | [[Category: CME]] | ||
[[Category: FAD]] | [[Category: FAD]] | ||
| Line 36: | Line 36: | ||
[[Category: tscp]] | [[Category: tscp]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:48:01 2008'' |
Revision as of 14:48, 21 February 2008
|
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 and 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
Page seeded by OCA on Thu Feb 21 16:48:01 2008
Categories: Paramecium bursaria chlorella virus 1 | Protein complex | Thymidylate synthase (FAD) | 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
