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2cfa
From Proteopedia
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| - | [[Image:2cfa.gif|left|200px]]<br /> | ||
| - | <applet load="2cfa" size="450" color="white" frame="true" align="right" spinBox="true" | ||
| - | caption="2cfa, resolution 2.30Å" /> | ||
| - | '''STRUCTURE OF VIRAL FLAVIN-DEPENDANT THYMIDYLATE SYNTHASE THYX'''<br /> | ||
| - | == | + | ==Structure of viral flavin-dependant thymidylate synthase ThyX== |
| - | By using biochemical and structural analyses, we have investigated the | + | <StructureSection load='2cfa' size='340' side='right'caption='[[2cfa]], [[Resolution|resolution]] 2.30Å' scene=''> |
| + | == Structural highlights == | ||
| + | <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='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='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='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> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/THYX_PBCV1 THYX_PBCV1] Catalyzes the formation of dTMP and tetrahydrofolate from dUMP and methylenetetrahydrofolate (By similarity). | ||
| + | == Evolutionary Conservation == | ||
| + | [[Image:Consurf_key_small.gif|200px|right]] | ||
| + | Check<jmol> | ||
| + | <jmolCheckbox> | ||
| + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/cf/2cfa_consurf.spt"</scriptWhenChecked> | ||
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
| + | <text>to colour the structure by Evolutionary Conservation</text> | ||
| + | </jmolCheckbox> | ||
| + | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2cfa ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == 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<ref>PMID:16707489</ref> | |
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| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 2cfa" style="background-color:#fffaf0;"></div> | |
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| - | + | ==See Also== | |
| + | *[[Thymidylate synthase 3D structures|Thymidylate synthase 3D structures]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Paramecium bursaria Chlorella virus 1]] | ||
| + | [[Category: Bernauer J]] | ||
| + | [[Category: Decottignies P]] | ||
| + | [[Category: Graille M]] | ||
| + | [[Category: Graziani S]] | ||
| + | [[Category: Liebl U]] | ||
| + | [[Category: Marchand C]] | ||
| + | [[Category: Myllykallio H]] | ||
| + | [[Category: Skouloubris S]] | ||
| + | [[Category: Zhou C-Z]] | ||
| + | [[Category: Van Tilbeurgh H]] | ||
Current revision
Structure of viral flavin-dependant thymidylate synthase ThyX
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