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| | <StructureSection load='2jmu' size='340' side='right'caption='[[2jmu]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | | <StructureSection load='2jmu' size='340' side='right'caption='[[2jmu]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2jmu]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JMU OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2JMU FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2jmu]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JMU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2JMU FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Thtpa ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice])</td></tr> | + | </td></tr><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=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/Thiamine-triphosphatase Thiamine-triphosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.1.28 3.6.1.28] </span></td></tr> | + | <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> |
| - | <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=2jmu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2jmu OCA], [http://pdbe.org/2jmu PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2jmu RCSB], [http://www.ebi.ac.uk/pdbsum/2jmu PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2jmu ProSAT], [http://www.topsan.org/Proteins/CESG/2jmu TOPSAN]</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=2jmu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2jmu OCA], [https://pdbe.org/2jmu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2jmu RCSB], [https://www.ebi.ac.uk/pdbsum/2jmu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2jmu ProSAT], [https://www.topsan.org/Proteins/CESG/2jmu TOPSAN]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/THTPA_MOUSE THTPA_MOUSE]] Hydrolase highly specific for thiamine triphosphate (ThTP) (By similarity). | + | [[https://www.uniprot.org/uniprot/THTPA_MOUSE THTPA_MOUSE]] Hydrolase highly specific for thiamine triphosphate (ThTP) (By similarity). |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
| Structural highlights
Function
[THTPA_MOUSE] Hydrolase highly specific for thiamine triphosphate (ThTP) (By similarity).
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Mammalian soluble thiamine triphosphatase (ThTPase) is a 25-kDa cytosolic enzyme that specifically catalyzes the conversion of thiamine triphosphate (ThTP) to thiamine diphosphate and has an absolute requirement for divalent cations. We have investigated the kinetic properties of recombinant mouse thiamine triphosphatase (mThTPase) and determined its solution structure by NMR spectroscopy. Residues responsible for binding Mg(2+) and ThTP were determined from NMR titration experiments. The binding of Mg(2+) induced only a minor local conformational change, whereas ThTP binding was found to cause a more global conformational change. We derived a structural model for the mThTPase.ThTP.Mg(2+) ternary complex and concluded from this that whereas free mThTPase has an open cleft fold, the enzyme in the ternary complex adopts a tunnel fold. Our results provide a functional rationale for a number of conserved residues and suggest an essential role for Mg(2+) in catalysis. We propose a mechanism underlying the high substrate specificity of mThTPase and discuss the possible role of water molecules in enzymatic catalysis.
Structural basis for the catalytic mechanism of mammalian 25-kDa thiamine triphosphatase.,Song J, Bettendorff L, Tonelli M, Markley JL J Biol Chem. 2008 Apr 18;283(16):10939-48. Epub 2008 Feb 14. PMID:18276586[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Song J, Bettendorff L, Tonelli M, Markley JL. Structural basis for the catalytic mechanism of mammalian 25-kDa thiamine triphosphatase. J Biol Chem. 2008 Apr 18;283(16):10939-48. Epub 2008 Feb 14. PMID:18276586 doi:10.1074/jbc.M709675200
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