2cfa: Difference between revisions
No edit summary |
No edit summary |
||
| Line 4: | Line 4: | ||
|PDB= 2cfa |SIZE=350|CAPTION= <scene name='initialview01'>2cfa</scene>, resolution 2.30Å | |PDB= 2cfa |SIZE=350|CAPTION= <scene name='initialview01'>2cfa</scene>, resolution 2.30Å | ||
|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> | ||
|LIGAND= <scene name='pdbligand=CME:S,S-(2-HYDROXYETHYL)THIOCYSTEINE'>CME</scene> | |LIGAND= <scene name='pdbligand=CME:S,S-(2-HYDROXYETHYL)THIOCYSTEINE'>CME</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene> | ||
|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] | |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= | ||
|DOMAIN= | |||
|RELATEDENTRY= | |||
|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> | |||
}} | }} | ||
| Line 33: | Line 36: | ||
[[Category: Tilbeurgh, H Van.]] | [[Category: Tilbeurgh, H Van.]] | ||
[[Category: Zhou, C Z.]] | [[Category: Zhou, C Z.]] | ||
[[Category: fdt]] | [[Category: fdt]] | ||
[[Category: flavin dependent thymidylate synthase fad]] | [[Category: flavin dependent thymidylate synthase fad]] | ||
| Line 45: | Line 46: | ||
[[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 Mon Mar 31 02:20:39 2008'' | ||
Revision as of 23:20, 30 March 2008
| |||||||||||||
| 2cfa, resolution 2.30Å | |||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Sites: | AC1 | ||||||||||||
| Ligands: | CME, FAD | ||||||||||||
| 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
Page seeded by OCA on Mon Mar 31 02:20:39 2008
Proteopedia Page Contributors and Editors (what is this?)
- Pages with broken file links
- 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.
- Fdt
- Flavin dependent thymidylate synthase fad
- Flavoprotein
- Methyltransferase
- Nucleotide biosynthesis
- Paramecium bursaria chlorella virus-1
- Thyx
- Transferase
- Tscp