5m4z: Difference between revisions

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 <StructureSection load='5m4z' size='340' side='right'caption='[[5m4z]], [[Resolution|resolution]] 1.18&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[5m4z]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5M4Z OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5M4Z FirstGlance]. <br>
+<table><tr><td colspan='2'>[[5m4z]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Trisp Trisp]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5M4Z OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5M4Z FirstGlance]. <br>
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=7K8:[(2~{R},3~{S},5~{R})-5-[(4~{E})-4-hydroxyimino-2-oxidanylidene-1,3-diazinan-1-yl]-3-oxidanyl-oxolan-2-yl]methyl+dihydrogen+phosphate'>7K8</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</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 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='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ts, Tsp_03568 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=6334 TRISP])</td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5m4z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5m4z OCA], [http://pdbe.org/5m4z PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5m4z RCSB], [http://www.ebi.ac.uk/pdbsum/5m4z PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5m4z ProSAT]</span></td></tr>
+<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Thymidylate_synthase Thymidylate synthase], with EC number [https://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'>[https://proteopedia.org/fgij/fg.htm?mol=5m4z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5m4z OCA], [https://pdbe.org/5m4z PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5m4z RCSB], [https://www.ebi.ac.uk/pdbsum/5m4z PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5m4z ProSAT]</span></td></tr>
 </table>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Novel evidence is presented allowing further clarification of the mechanism of the slow-binding thymidylate synthase (TS) inhibition by N(4)-hydroxy-dCMP (N(4)-OH-dCMP). Spectrophotometric monitoring documented time- and temperature-, and N(4)-OH-dCMP-dependent TS-catalyzed dihydrofolate production, accompanying the mouse enzyme incubation with N(4)-OH-dCMP and N(5,10)-methylenetetrahydrofolate, known to inactivate the enzyme by the covalent binding of the inhibitor, suggesting the demonstrated reaction to be uncoupled from the pyrimidine C(5) methylation. The latter was in accord with the hypothesis based on the previously presented structure of mouse TS (cf. PDB ID: 4EZ8), and with conclusions based on the present structure of the parasitic nematode Trichinella spiralis, both co-crystallized with N(4)-OH-dCMP and N(5,10)-methylenetetrahdrofolate. The crystal structure of the mouse TS-N(4)-OH-dCMP complex soaked with N(5,10)-methylenetetrahydrofolate revealed the reaction to run via a unique imidazolidine ring opening, leaving the one-carbon group bound to the N(10) atom, thus too distant from the pyrimidine C(5) atom to enable the electrophilic attack and methylene group transfer.
+Molecular Mechanism of Thymidylate Synthase Inhibition by N(4)-Hydroxy-dCMP in View of Spectrophotometric and Crystallographic Studies.,Maj P, Jarmula A, Wilk P, Prokopowicz M, Rypniewski W, Zielinski Z, Dowiercial A, Bzowska A, Rode W Int J Mol Sci. 2021 Apr 30;22(9). pii: ijms22094758. doi: 10.3390/ijms22094758. PMID:33946210<ref>PMID:33946210</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 5m4z" style="background-color:#fffaf0;"></div>
 ==See Also==
 *[[Thymidylate synthase 3D structures|Thymidylate synthase 3D structures]]
+== References ==
+<references/>
 __TOC__
 </StructureSection>
 [[Category: Large Structures]]
 [[Category: Thymidylate synthase]]
+[[Category: Trisp]]
 [[Category: Dowiercial, A]]
 [[Category: Jarmula, A]]