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3tvl

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<StructureSection load='3tvl' size='340' side='right'caption='[[3tvl]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
<StructureSection load='3tvl' size='340' side='right'caption='[[3tvl]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3tvl]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3TVL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3TVL FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3tvl]] is a 2 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=3TVL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3TVL FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=3PO:TRIPHOSPHATE'>3PO</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</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]] 2.3&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3bhd|3bhd]], [[2jmu|2jmu]]</div></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=3PO:TRIPHOSPHATE'>3PO</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">THTPA ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Thiamine-triphosphatase Thiamine-triphosphatase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.1.28 3.6.1.28] </span></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=3tvl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3tvl OCA], [https://pdbe.org/3tvl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3tvl RCSB], [https://www.ebi.ac.uk/pdbsum/3tvl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3tvl ProSAT]</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=3tvl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3tvl OCA], [https://pdbe.org/3tvl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3tvl RCSB], [https://www.ebi.ac.uk/pdbsum/3tvl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3tvl ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/THTPA_HUMAN THTPA_HUMAN]] Hydrolase highly specific for thiamine triphosphate (ThTP).
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[https://www.uniprot.org/uniprot/THTPA_HUMAN THTPA_HUMAN] Hydrolase highly specific for thiamine triphosphate (ThTP).
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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BACKGROUND: Thiamine triphosphate (ThTP) is present in most organisms and might be involved in intracellular signaling. In mammalian cells, the cytosolic ThTP level is controlled by a specific thiamine triphosphatase (ThTPase), belonging to the CYTH superfamily of proteins. CYTH proteins are present in all superkingdoms of life and act on various triphosphorylated substrates. METHODS: Using crystallography, mass spectrometry and mutational analysis, we identified the key structural determinants of the high specificity and catalytic efficiency of mammalian ThTPase. RESULTS: Triphosphate binding requires three conserved arginines while the catalytic mechanism relies on an unusual lysine-tyrosine dyad. By docking of the ThTP molecule in the active site, we found that Trp-53 should interact with the thiazole part of the substrate molecule, thus playing a key role in substrate recognition and specificity. Sea anemone and zebrafish CYTH proteins, which retain the corresponding Trp residue, are also specific ThTPases. Surprisingly, the whole chromosome region containing the ThTPase gene is lost in birds. CONCLUSIONS: The specificity for ThTP is linked to a stacking interaction between the thiazole heterocycle of thiamine and a tryptophan residue. The latter likely plays a key role in the secondary acquisition of ThTPase activity in early metazoan CYTH enzymes, in the lineage leading from cnidarians to mammals. GENERAL SIGNIFICANCE: We show that ThTPase activity is not restricted to mammals as previously thought but is an acquisition of early metazoans. This, and the identification of critically important residues, allows us to draw an evolutionary perspective of the CYTH family of proteins.
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Structural determinants of specificity and catalytic mechanism in mammalian 25-kDa thiamine triphosphatase.,Delvaux D, Kerff F, Murty MR, Lakaye B, Czerniecki J, Kohn G, Wins P, Herman R, Gabelica V, Heuze F, Tordoir X, Maree R, Matagne A, Charlier P, De Pauw E, Bettendorff L Biochim Biophys Acta. 2013 May 22. pii: S0304-4165(13)00210-9. doi:, 10.1016/j.bbagen.2013.05.014. PMID:23707715<ref>PMID:23707715</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 3tvl" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Human]]
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[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Thiamine-triphosphatase]]
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[[Category: Bettendorff L]]
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[[Category: Bettendorff, L]]
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[[Category: Charlier P]]
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[[Category: Charlier, P]]
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[[Category: Delvaux D]]
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[[Category: Delvaux, D]]
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[[Category: Herman R]]
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[[Category: Herman, R]]
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[[Category: Kerff F]]
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[[Category: Kerff, F]]
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[[Category: Sauvage E]]
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[[Category: Sauvage, E]]
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[[Category: Wins P]]
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[[Category: Wins, P]]
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[[Category: Hydrolase]]
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[[Category: Magnesium binding]]
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Current revision

Complex between the human thiamine triphosphatase and triphosphate

PDB ID 3tvl

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