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| | ==Crystal structure of Triosephosphate Isomerase from Clostridium perfringens== | | ==Crystal structure of Triosephosphate Isomerase from Clostridium perfringens== |
| - | <StructureSection load='4y8f' size='340' side='right' caption='[[4y8f]], [[Resolution|resolution]] 1.54Å' scene=''> | + | <StructureSection load='4y8f' size='340' side='right'caption='[[4y8f]], [[Resolution|resolution]] 1.54Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4y8f]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4Y8F OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4Y8F FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4y8f]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Clostridium_perfringens_str._13 Clostridium perfringens str. 13]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4Y8F OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4Y8F FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</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]] 1.54Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4y90|4y90]], [[4y96|4y96]], [[4y9a|4y9a]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</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=4y8f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4y8f OCA], [https://pdbe.org/4y8f PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4y8f RCSB], [https://www.ebi.ac.uk/pdbsum/4y8f PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4y8f 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=4y8f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4y8f OCA], [http://pdbe.org/4y8f PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4y8f RCSB], [http://www.ebi.ac.uk/pdbsum/4y8f PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4y8f ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/TPIS_CLOPE TPIS_CLOPE] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </div> | | </div> |
| | <div class="pdbe-citations 4y8f" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 4y8f" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Triose phosphate isomerase 3D structures|Triose phosphate isomerase 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Triose-phosphate isomerase]] | + | [[Category: Clostridium perfringens str. 13]] |
| - | [[Category: Fernandez-Velasco, D A]] | + | [[Category: Large Structures]] |
| - | [[Category: Rodriguez-Romero, A]] | + | [[Category: Fernandez-Velasco DA]] |
| - | [[Category: Romero-Romero, S]] | + | [[Category: Rodriguez-Romero A]] |
| - | [[Category: Isomerase]]
| + | [[Category: Romero-Romero S]] |
| - | [[Category: Tim barrel]]
| + | |
| - | [[Category: Tpi]]
| + | |
| Structural highlights
Function
TPIS_CLOPE
Publication Abstract from PubMed
Temperature is one of the main variables that modulate protein function and stability. Thermodynamic studies of oligomeric proteins, the dominant protein natural form, have been often hampered because irreversible aggregation and/or slow reactions are common. There are no reports on the reversible equilibrium thermal unfolding of proteins composed of (beta/alpha)8 barrel subunits, albeit this "TIM barrel" topology is one of the most abundant and versatile in nature. We studied the eponymous TIM barrel, triosephosphate isomerase (TIM), belonging to five species of different bacterial taxa. All of them were found to be catalytically efficient dimers. The three-dimensional structure of four enzymes was solved at high/medium resolution. Irreversibility and kinetic control were observed in the thermal unfolding of two TIMs, while for the other three the thermal unfolding was found to follow a two-state equilibrium reversible process. Shifts in the global stability curves of these three proteins are related to the organismal temperature range of optimal growth and modulated by variations in maximum stability temperature and in the enthalpy change at that temperature. Reversibility appears to correlate with the low isoelectric point, the absence of a residual structure in the unfolded state, small cavity volume in the native state, low conformational stability and a low melting temperature. Furthermore, the strong coupling between dimer dissociation and monomer unfolding may reduce aggregation and favour reversibility. It is therefore very thought-provoking to find that a common topological ensemble, such as the TIM barrel, can unfold/refold in the Anfinsen way, i.e. without the help of the cellular machinery.
Reversibility and two state behaviour in the thermal unfolding of oligomeric TIM barrel proteins.,Romero-Romero S, Costas M, Rodriguez-Romero A, Alejandro Fernandez-Velasco D Phys Chem Chem Phys. 2015 Jul 24. PMID:26206330[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Romero-Romero S, Costas M, Rodriguez-Romero A, Alejandro Fernandez-Velasco D. Reversibility and two state behaviour in the thermal unfolding of oligomeric TIM barrel proteins. Phys Chem Chem Phys. 2015 Jul 24. PMID:26206330 doi:http://dx.doi.org/10.1039/c5cp01599e
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