6cg9: Difference between revisions
New page: '''Unreleased structure''' The entry 6cg9 is ON HOLD until Paper Publication Authors: Romero-Romero, S., Fernandez-Velasco, D.A., Rodriguez-Romero, A. Description: Crystal structure of... |
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==Crystal structure of Triosephosphate Isomerase from Zea mays (mexican corn)== | |||
<StructureSection load='6cg9' size='340' side='right'caption='[[6cg9]], [[Resolution|resolution]] 1.80Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6cg9]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Zea_mays Zea mays]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6CG9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6CG9 FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8Å</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=GOL:GLYCEROL'>GOL</scene></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=6cg9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6cg9 OCA], [https://pdbe.org/6cg9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6cg9 RCSB], [https://www.ebi.ac.uk/pdbsum/6cg9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6cg9 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/TPIS_MAIZE TPIS_MAIZE] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
We studied the structure, function and thermodynamic properties for the unfolding of the Triosephosphate isomerase (TIM) from Zea mays (ZmTIM). ZmTIM shows a catalytic efficiency close to the diffusion limit. Native ZmTIM is a dimer that dissociates upon dilution into inactive and unfolded monomers. Its thermal unfolding is irreversible with a Tm of 61.6+/-1.4 degrees C and an activation energy of 383.4+/-11.5kJmol(-1). The urea-induced unfolding of ZmTIM is reversible. Transitions followed by catalytic activity and spectroscopic properties are monophasic and superimposable, indicating that ZmTIM unfolds/refolds in a two-state behavior with an unfolding DeltaG degrees (H20)=99.8+/-5.3kJmol(-1). This contrasts with most other studied TIMs, where folding intermediates are common. The three-dimensional structure of ZmTIM was solved at 1.8A. A structural comparison with other eukaryotic TIMs shows a similar number of intramolecular and intermolecular interactions. Interestingly the number of interfacial water molecules found in ZmTIM is lower than those observed in most TIMs that show folding intermediates. Although with the available data, there is no clear correlation between structural properties and the number of equilibrium intermediates in the unfolding of TIM, the identification of such structural properties should increase our understanding of folding mechanisms. | |||
Structure and conformational stability of the triosephosphate isomerase from Zea mays. Comparison with the chemical unfolding pathways of other eukaryotic TIMs.,Romero-Romero S, Becerril-Sesin LA, Costas M, Rodriguez-Romero A, Fernandez-Velasco DA Arch Biochem Biophys. 2018 Sep 24;658:66-76. doi: 10.1016/j.abb.2018.09.022. PMID:30261166<ref>PMID:30261166</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: Fernandez-Velasco | <div class="pdbe-citations 6cg9" style="background-color:#fffaf0;"></div> | ||
[[Category: | |||
[[Category: | ==See Also== | ||
*[[Triose phosphate isomerase 3D structures|Triose phosphate isomerase 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Zea mays]] | |||
[[Category: Fernandez-Velasco DA]] | |||
[[Category: Rodriguez-Romero A]] | |||
[[Category: Romero-Romero S]] | |||
Latest revision as of 18:04, 4 October 2023
Crystal structure of Triosephosphate Isomerase from Zea mays (mexican corn)Crystal structure of Triosephosphate Isomerase from Zea mays (mexican corn)
Structural highlights
FunctionPublication Abstract from PubMedWe studied the structure, function and thermodynamic properties for the unfolding of the Triosephosphate isomerase (TIM) from Zea mays (ZmTIM). ZmTIM shows a catalytic efficiency close to the diffusion limit. Native ZmTIM is a dimer that dissociates upon dilution into inactive and unfolded monomers. Its thermal unfolding is irreversible with a Tm of 61.6+/-1.4 degrees C and an activation energy of 383.4+/-11.5kJmol(-1). The urea-induced unfolding of ZmTIM is reversible. Transitions followed by catalytic activity and spectroscopic properties are monophasic and superimposable, indicating that ZmTIM unfolds/refolds in a two-state behavior with an unfolding DeltaG degrees (H20)=99.8+/-5.3kJmol(-1). This contrasts with most other studied TIMs, where folding intermediates are common. The three-dimensional structure of ZmTIM was solved at 1.8A. A structural comparison with other eukaryotic TIMs shows a similar number of intramolecular and intermolecular interactions. Interestingly the number of interfacial water molecules found in ZmTIM is lower than those observed in most TIMs that show folding intermediates. Although with the available data, there is no clear correlation between structural properties and the number of equilibrium intermediates in the unfolding of TIM, the identification of such structural properties should increase our understanding of folding mechanisms. Structure and conformational stability of the triosephosphate isomerase from Zea mays. Comparison with the chemical unfolding pathways of other eukaryotic TIMs.,Romero-Romero S, Becerril-Sesin LA, Costas M, Rodriguez-Romero A, Fernandez-Velasco DA Arch Biochem Biophys. 2018 Sep 24;658:66-76. doi: 10.1016/j.abb.2018.09.022. PMID:30261166[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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