6CG9

Crystal structure of Triosephosphate Isomerase from Zea mays (mexican corn)

Summary for 6CG9

• Entry DOI: 10.2210/pdb6cg9/pdb
• Descriptor: Triosephosphate isomerase, cytosolic, GLYCEROL, ACETATE ION, ... (4 entities in total)
• Functional Keywords: isomerase, glycolysis, tim-barrel
• Biological source: Zea mays (Maize)
• Total number of polymer chains: 2
• Total formula weight: 54819.35

Authors

Romero-Romero, S.,Fernandez-Velasco, D.A.,Rodriguez-Romero, A. (deposition date: 2018-02-19, release date: 2018-10-10, Last modification date: 2023-10-04)

Primary citation

Romero-Romero, S.,Becerril-Sesin, L.A.,Costas, M.,Rodriguez-Romero, A.,Fernandez-Velasco, D.A.
Structure and conformational stability of the triosephosphate isomerase from Zea mays. Comparison with the chemical unfolding pathways of other eukaryotic TIMs.
Arch. Biochem. Biophys., 658:66-76, 2018

PubMed Abstract: 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 T of 61.6 ± 1.4 °C and an activation energy of 383.4 ± 11.5 kJ mol. 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 ΔG° = 99.8 ± 5.3 kJ mol. This contrasts with most other studied TIMs, where folding intermediates are common. The three-dimensional structure of ZmTIM was solved at 1.8 Å. 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.

PubMed: 30261166
DOI: 10.1016/j.abb.2018.09.022

Experimental method

X-RAY DIFFRACTION (1.8 Å)