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| | <StructureSection load='4hhp' size='340' side='right'caption='[[4hhp]], [[Resolution|resolution]] 1.50Å' scene=''> | | <StructureSection load='4hhp' size='340' side='right'caption='[[4hhp]], [[Resolution|resolution]] 1.50Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4hhp]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Trycr Trycr]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4HHP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4HHP FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4hhp]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Trypanosoma_cruzi Trypanosoma cruzi]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4HHP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4HHP FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.5Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1tcd|1tcd]], [[1ci1|1ci1]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Triose-phosphate_isomerase Triose-phosphate isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.3.1.1 5.3.1.1] </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=4hhp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4hhp OCA], [https://pdbe.org/4hhp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4hhp RCSB], [https://www.ebi.ac.uk/pdbsum/4hhp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4hhp ProSAT]</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=4hhp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4hhp OCA], [http://pdbe.org/4hhp PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4hhp RCSB], [http://www.ebi.ac.uk/pdbsum/4hhp PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4hhp ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| - | <div style="background-color:#fffaf0;">
| + | == Function == |
| - | == Publication Abstract from PubMed == | + | [https://www.uniprot.org/uniprot/TPIS_TRYCR TPIS_TRYCR] |
| - | It is generally assumed that the amino acids that exist in all homologous enzymes correspond to residues that participate in catalysis, or that are essential for folding and stability. Although this holds for catalytic residues, the function of conserved non-catalytic residues is not clear. It is not known if such residues are of equal importance and have the same role in different homologous enzymes. In humans, the E104D mutation in triosephosphate isomerase (TIM) is the most frequent mutation in the autosomal diseases named "TPI deficiencies". We explored if the E104D mutation has the same impact in TIMs from four different organisms (Homo sapiens, Giardia lamblia, Trypanosoma cruzi, T. brucei). The catalytic properties were not significantly affected by the mutation, but it affected the rate and extent of formation of active dimers from unfolded monomers differently. Scanning calorimetry experiments indicated that the mutation was in all cases destabilizing, but the mutation effect on rates of irreversible denaturation and transition-state energetics were drastically dependent on the TIM background. For instance, mutational changes in activation energy ranged from 430 kJ mol-1 in HsTIM to -78 kJ mol-1 in TcTIM. Thus, in TIM the role of a conserved non-catalytic residue is drastically dependent on its molecular background. Accordingly, it would seem that because each protein has a particular sequence, and a distinctive set of amino acid interactions, it should be regarded as a unique entity that has evolved for function and stability in the organisms to which it belongs. (c) Proteins 2013;. (c) 2013 Wiley Periodicals, Inc.
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| - | Different contribution of conserved amino acids to the global properties of Triosephosphate isomerases.,Aguirre Y, Cabrera N, Aguirre B, Perez-Montfort R, Hernandez-Santoyo A, Reyes-Vivas H, Enriquez-Flores S, de Gomez-Puyou MT, Gomez-Puyou A, Sanchez-Ruiz JM, Costas M Proteins. 2013 Aug 22. doi: 10.1002/prot.24398. PMID:23966267<ref>PMID:23966267</ref>
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| - | </div>
| + | |
| - | <div class="pdbe-citations 4hhp" style="background-color:#fffaf0;"></div>
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| | | | |
| | ==See Also== | | ==See Also== |
| - | *[[Triose Phosphate Isomerase|Triose Phosphate Isomerase]] | + | *[[Triose phosphate isomerase 3D structures|Triose phosphate isomerase 3D structures]] |
| - | == References ==
| + | |
| - | <references/>
| + | |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Triose-phosphate isomerase]] | + | [[Category: Trypanosoma cruzi]] |
| - | [[Category: Trycr]]
| + | [[Category: Aguirre-Fuentes Y]] |
| - | [[Category: Aguirre-Fuentes, Y]] | + | [[Category: De Gomez-Puyou MT]] |
| - | [[Category: Gomez-Puyou, A]] | + | [[Category: Gomez-Puyou A]] |
| - | [[Category: Gomez-Puyou, M T.De]] | + | [[Category: Hernandez-Santoyo A]] |
| - | [[Category: Hernandez-Santoyo, A]] | + | [[Category: Torres-Larios A]] |
| - | [[Category: Torres-Larios, A]] | + | |
| - | [[Category: Disease mutation]]
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| - | [[Category: Gluconeogenesis]]
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| - | [[Category: Glycolysis]]
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| - | [[Category: Isomerase]]
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| - | [[Category: Pentose shunt]]
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| - | [[Category: Tim barrel]]
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