2cfa

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|PDB= 2cfa |SIZE=350|CAPTION= <scene name='initialview01'>2cfa</scene>, resolution 2.30&Aring;
|PDB= 2cfa |SIZE=350|CAPTION= <scene name='initialview01'>2cfa</scene>, resolution 2.30&Aring;
|SITE= <scene name='pdbsite=AC1:Fad+Binding+Site+For+Chain+B'>AC1</scene>
|SITE= <scene name='pdbsite=AC1:Fad+Binding+Site+For+Chain+B'>AC1</scene>
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|LIGAND= <scene name='pdbligand=CME:S,S-(2-HYDROXYETHYL)THIOCYSTEINE'>CME</scene> and <scene name='pdbligand=FAD:FLAVIN-ADENINE DINUCLEOTIDE'>FAD</scene>
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|LIGAND= <scene name='pdbligand=CME:S,S-(2-HYDROXYETHYL)THIOCYSTEINE'>CME</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>
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|ACTIVITY= [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]
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|ACTIVITY= <span class='plainlinks'>[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] </span>
|GENE=
|GENE=
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|DOMAIN=
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2cfa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2cfa OCA], [http://www.ebi.ac.uk/pdbsum/2cfa PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2cfa RCSB]</span>
}}
}}
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[[Category: Tilbeurgh, H Van.]]
[[Category: Tilbeurgh, H Van.]]
[[Category: Zhou, C Z.]]
[[Category: Zhou, C Z.]]
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[[Category: CME]]
 
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[[Category: FAD]]
 
[[Category: fdt]]
[[Category: fdt]]
[[Category: flavin dependent thymidylate synthase fad]]
[[Category: flavin dependent thymidylate synthase fad]]
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[[Category: tscp]]
[[Category: tscp]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 16:14:37 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 02:20:39 2008''

Revision as of 23:20, 30 March 2008

Image:2cfa.gif


PDB ID 2cfa

Drag the structure with the mouse to rotate
, resolution 2.30Å
Sites:
Ligands: ,
Activity: Thymidylate synthase (FAD), with EC number 2.1.1.148
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



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. 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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