2jmu

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{{Seed}}
 
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[[Image:2jmu.png|left|200px]]
 
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==NMR structure of the mouse thiamine triphosphatase==
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The line below this paragraph, containing "STRUCTURE_2jmu", creates the "Structure Box" on the page.
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<StructureSection load='2jmu' size='340' side='right'caption='[[2jmu]]' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[2jmu]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. 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>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=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>
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{{STRUCTURE_2jmu| PDB=2jmu | SCENE= }}
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/THTPA_MOUSE THTPA_MOUSE] Hydrolase highly specific for thiamine triphosphate (ThTP) (By similarity).
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/jm/2jmu_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2jmu ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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===NMR structure of the mouse thiamine triphosphatase===
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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<ref>PMID:18276586</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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The line below this paragraph, {{ABSTRACT_PUBMED_18276586}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 2jmu" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 18276586 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_18276586}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[Category: Large Structures]]
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2JMU is a 1 chain structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JMU OCA].
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==Reference==
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<ref group="xtra">PMID:18276586</ref><references group="xtra"/>
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[[Category: Mus musculus]]
[[Category: Mus musculus]]
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[[Category: Thiamine-triphosphatase]]
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[[Category: Markley JL]]
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[[Category: CESG, Center for Eukaryotic Structural Genomics.]]
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[[Category: Song J]]
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[[Category: Markley, J L.]]
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[[Category: Song, J.]]
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[[Category: Center for eukaryotic structural genomic]]
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[[Category: Cesg]]
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[[Category: Hydrolase]]
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[[Category: Protein structure initiative]]
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[[Category: Psi]]
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[[Category: Structural genomic]]
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[[Category: Thiamine triphosphatase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jun 10 20:27:50 2009''
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Current revision

NMR structure of the mouse thiamine triphosphatase

PDB ID 2jmu

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Proteopedia Page Contributors and Editors (what is this?)

OCA

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