2cfa
From Proteopedia
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| - | [[Image:2cfa.gif|left|200px]]<br /><applet load="2cfa" size=" | + | [[Image:2cfa.gif|left|200px]]<br /><applet load="2cfa" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="2cfa, resolution 2.30Å" /> | caption="2cfa, resolution 2.30Å" /> | ||
'''STRUCTURE OF VIRAL FLAVIN-DEPENDANT THYMIDYLATE SYNTHASE THYX'''<br /> | '''STRUCTURE OF VIRAL FLAVIN-DEPENDANT THYMIDYLATE SYNTHASE THYX'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2CFA is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Paramecium_bursaria_chlorella_virus_1 Paramecium bursaria chlorella virus 1] with CME and FAD as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Thymidylate_synthase_(FAD) Thymidylate synthase (FAD)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.148 2.1.1.148] Known structural/functional Site: <scene name='pdbsite=AC1:Fad Binding Site For Chain B'>AC1</scene>. Full crystallographic information is available from [http:// | + | 2CFA is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Paramecium_bursaria_chlorella_virus_1 Paramecium bursaria chlorella virus 1] with <scene name='pdbligand=CME:'>CME</scene> and <scene name='pdbligand=FAD:'>FAD</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Thymidylate_synthase_(FAD) Thymidylate synthase (FAD)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.148 2.1.1.148] Known structural/functional Site: <scene name='pdbsite=AC1:Fad+Binding+Site+For+Chain+B'>AC1</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CFA OCA]. |
==Reference== | ==Reference== | ||
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[[Category: tscp]] | [[Category: tscp]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb 3 10:34:38 2008'' |
Revision as of 08:34, 3 February 2008
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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, 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
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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
