4eb4: Difference between revisions
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==Crystal structure of mouse thymidylate synthase in ternary complex with dUMP and Tomudex== | ==Crystal structure of mouse thymidylate synthase in ternary complex with dUMP and Tomudex== | ||
<StructureSection load='4eb4' size='340' side='right' caption='[[4eb4]], [[Resolution|resolution]] 1.74Å' scene=''> | <StructureSection load='4eb4' size='340' side='right' caption='[[4eb4]], [[Resolution|resolution]] 1.74Å' scene=''> | ||
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Tyms ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice])</td></tr> | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Tyms ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice])</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 Thymidylate synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.45 2.1.1.45] </span></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 Thymidylate synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.45 2.1.1.45] </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=4eb4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4eb4 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4eb4 RCSB], [http://www.ebi.ac.uk/pdbsum/4eb4 PDBsum]</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=4eb4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4eb4 OCA], [http://pdbe.org/4eb4 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4eb4 RCSB], [http://www.ebi.ac.uk/pdbsum/4eb4 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4eb4 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 4eb4" style="background-color:#fffaf0;"></div> | |||
==See Also== | ==See Also== | ||
Revision as of 20:36, 9 March 2017
Crystal structure of mouse thymidylate synthase in ternary complex with dUMP and TomudexCrystal structure of mouse thymidylate synthase in ternary complex with dUMP and Tomudex
Structural highlights
Function[TYSY_MOUSE] Contributes to the de novo mitochondrial thymidylate biosynthesis pathway (By similarity). Publication Abstract from PubMedThe crystal structure of mouse thymidylate synthase (mTS) in complex with substrate dUMP and antifolate inhibitor Raltitrexed is reported. The structure reveals, for the first time in the group of mammalian TS structures, a well-ordered segment of 13 N-terminal amino acids, whose ordered conformation is stabilized due to specific crystal packing. The structure consists of two homodimers, differing in conformation, one being more closed (dimer AB) and thus supporting tighter binding of ligands, and the other being more open (dimer CD) and thus allowing weaker binding of ligands. This difference indicates an asymmetrical effect of the binding of Raltitrexed to two independent mTS molecules. Conformational changes leading to a ligand-induced closing of the active site cleft are observed by comparing the crystal structures of mTS in three different states along the catalytic pathway: ligand-free, dUMP-bound, and dUMP- and Raltitrexed-bound. Possible interaction routes between hydrophobic residues of the mTS protein N-terminal segment and the active site are also discussed. Crystal structure of mouse thymidylate synthase in tertiary complex with dUMP and raltitrexed reveals N-terminus architecture and two different active site conformations.,Dowiercial A, Wilk P, Rypniewski W, Rode W, Jarmula A Biomed Res Int. 2014;2014:945803. doi: 10.1155/2014/945803. Epub 2014 Jun 3. PMID:24995339[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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