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| | <StructureSection load='2cfa' size='340' side='right'caption='[[2cfa]], [[Resolution|resolution]] 2.30Å' scene=''> | | <StructureSection load='2cfa' size='340' side='right'caption='[[2cfa]], [[Resolution|resolution]] 2.30Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2cfa]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Chlorella_pbcv-1_virus Chlorella pbcv-1 virus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CFA OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2CFA FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2cfa]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Paramecium_bursaria_Chlorella_virus_1 Paramecium bursaria Chlorella virus 1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CFA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2CFA FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3Å</td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=CME:S,S-(2-HYDROXYETHYL)THIOCYSTEINE'>CME</scene></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CME:S,S-(2-HYDROXYETHYL)THIOCYSTEINE'>CME</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><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></td></tr>
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2cfa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2cfa OCA], [https://pdbe.org/2cfa PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2cfa RCSB], [https://www.ebi.ac.uk/pdbsum/2cfa PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2cfa ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><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://pdbe.org/2cfa PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2cfa RCSB], [http://www.ebi.ac.uk/pdbsum/2cfa PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2cfa ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/THYX_PBCV1 THYX_PBCV1]] Catalyzes the formation of dTMP and tetrahydrofolate from dUMP and methylenetetrahydrofolate (By similarity). | + | [https://www.uniprot.org/uniprot/THYX_PBCV1 THYX_PBCV1] Catalyzes the formation of dTMP and tetrahydrofolate from dUMP and methylenetetrahydrofolate (By similarity). |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | ==See Also== | | ==See Also== |
| - | *[[Thymidylate synthase|Thymidylate synthase]] | + | *[[Thymidylate synthase 3D structures|Thymidylate synthase 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Chlorella pbcv-1 virus]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Bernauer, J]] | + | [[Category: Paramecium bursaria Chlorella virus 1]] |
| - | [[Category: Decottignies, P]] | + | [[Category: Bernauer J]] |
| - | [[Category: Graille, M]] | + | [[Category: Decottignies P]] |
| - | [[Category: Graziani, S]] | + | [[Category: Graille M]] |
| - | [[Category: Liebl, U]] | + | [[Category: Graziani S]] |
| - | [[Category: Marchand, C]] | + | [[Category: Liebl U]] |
| - | [[Category: Myllykallio, H]] | + | [[Category: Marchand C]] |
| - | [[Category: Skouloubris, S]] | + | [[Category: Myllykallio H]] |
| - | [[Category: Tilbeurgh, H van]]
| + | [[Category: Skouloubris S]] |
| - | [[Category: Zhou, C Z]] | + | [[Category: Zhou C-Z]] |
| - | [[Category: Fdt]] | + | [[Category: Van Tilbeurgh H]] |
| - | [[Category: Flavin dependent thymidylate synthase fad]]
| + | |
| - | [[Category: Flavoprotein]]
| + | |
| - | [[Category: Methyltransferase]]
| + | |
| - | [[Category: Nucleotide biosynthesis]]
| + | |
| - | [[Category: Transferase]]
| + | |
| - | [[Category: Tscp]]
| + | |
| Structural highlights
Function
THYX_PBCV1 Catalyzes the formation of dTMP and tetrahydrofolate from dUMP and methylenetetrahydrofolate (By similarity).
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Graziani S, Bernauer J, Skouloubris S, Graille M, Zhou CZ, Marchand C, Decottignies P, van Tilbeurgh H, Myllykallio H, Liebl U. Catalytic mechanism and structure of viral flavin-dependent thymidylate synthase ThyX. J Biol Chem. 2006 Aug 18;281(33):24048-57. Epub 2006 May 17. PMID:16707489 doi:10.1074/jbc.M600745200
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