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4h1i

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==Structure of human thymidylate synthase at low salt conditions==
==Structure of human thymidylate synthase at low salt conditions==
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<StructureSection load='4h1i' size='340' side='right' caption='[[4h1i]], [[Resolution|resolution]] 3.10&Aring;' scene=''>
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<StructureSection load='4h1i' size='340' side='right'caption='[[4h1i]], [[Resolution|resolution]] 3.10&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4h1i]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4H1I OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4H1I FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4h1i]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4H1I OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4H1I FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.095&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4gyh|4gyh]]</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">TYMS, TS, OK/SW-cl.29 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4h1i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4h1i OCA], [https://pdbe.org/4h1i PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4h1i RCSB], [https://www.ebi.ac.uk/pdbsum/4h1i PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4h1i ProSAT]</span></td></tr>
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<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>
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<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=4h1i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4h1i OCA], [http://pdbe.org/4h1i PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4h1i RCSB], [http://www.ebi.ac.uk/pdbsum/4h1i PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4h1i ProSAT]</span></td></tr>
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</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/TYSY_HUMAN TYSY_HUMAN]] Contributes to the de novo mitochondrial thymidylate biosynthesis pathway.<ref>PMID:21876188</ref>
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[https://www.uniprot.org/uniprot/TYSY_HUMAN TYSY_HUMAN] Contributes to the de novo mitochondrial thymidylate biosynthesis pathway.<ref>PMID:21876188</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Expression of hTS (human thymidylate synthase), a key enzyme in thymidine biosynthesis, is regulated on the translational level through a feedback mechanism that is rarely found in eukaryotes. At low substrate concentrations, the ligand-free enzyme binds to its own mRNA and stabilizes a hairpin structure that sequesters the start codon. When in complex with dUMP (2'-deoxyuridine-5'-monophosphate) and a THF (tetrahydrofolate) cofactor, the enzyme adopts a conformation that is unable to bind and repress expression of mRNA. Here, we have used a combination of X-ray crystallography, RNA mutagenesis and site-specific cross-linking studies to investigate the molecular recognition of TS mRNA by the hTS enzyme. The interacting mRNA region was narrowed to the start codon and immediately flanking sequences. In the hTS enzyme, a helix-loop-helix domain on the protein surface was identified as the putative RNA-binding site.
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Analysis of mRNA recognition by human thymidylate synthase.,Brunn ND, Dibrov SM, Kao MB, Ghassemian M, Hermann T Biosci Rep. 2014 Dec 23;34(6). pii: e00168. doi: 10.1042/BSR20140137. PMID:25423174<ref>PMID:25423174</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 4h1i" style="background-color:#fffaf0;"></div>
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==See Also==
==See Also==
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*[[Thymidylate synthase|Thymidylate synthase]]
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*[[Thymidylate synthase 3D structures|Thymidylate synthase 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Human]]
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[[Category: Homo sapiens]]
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[[Category: Thymidylate synthase]]
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[[Category: Large Structures]]
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[[Category: Brunn, N]]
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[[Category: Brunn N]]
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[[Category: Dibrov, S]]
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[[Category: Dibrov S]]
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[[Category: Hermann, T]]
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[[Category: Hermann T]]
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[[Category: Cancer chemotherapy target]]
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[[Category: Methyl transferase]]
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[[Category: Nucleotide metabolism]]
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[[Category: Transferase]]
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Current revision

Structure of human thymidylate synthase at low salt conditions

PDB ID 4h1i

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