4OBT

Crystal structure of Arabidopsis thaliana cytosolic triose phosphate isomerase

4OBT の概要

• エントリーDOI: 10.2210/pdb4obt/pdb
• 分子名称: Triosephosphate isomerase, cytosolic (2 entities in total)
• 機能のキーワード: tim barrel, glycolysis, citosolyc, isomerase
• 由来する生物種: Arabidopsis thaliana (mouse-ear cress,thale-cress)
• 細胞内の位置: Cytoplasm : P48491
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 54978.64

構造登録者

Lopez-Castillo, M.,Jimenez-Sandoval, P.,Lara-Gonzalez, S.,Brieba, L.G.,Baruch, N. (登録日: 2014-01-07, 公開日: 2016-01-13, 最終更新日: 2024-02-28)

主引用文献

Lopez-Castillo, L.M.,Jimenez-Sandoval, P.,Baruch-Torres, N.,Trasvina-Arenas, C.H.,Diaz-Quezada, C.,Lara-Gonzalez, S.,Winkler, R.,Brieba, L.G.
Structural Basis for Redox Regulation of Cytoplasmic and Chloroplastic Triosephosphate Isomerases from Arabidopsis thaliana.
Front Plant Sci, 7:1817-1817, 2016

PubMed Abstract: In plants triosephosphate isomerase (TPI) interconverts glyceraldehyde 3-phosphate (G3P) and dihydroxyacetone phosphate (DHAP) during glycolysis, gluconeogenesis, and the Calvin-Benson cycle. The nuclear genome of land plants encodes two genes, one gene product is located in the cytoplasm and the other is imported into the chloroplast. Herein we report the crystal structures of the TPIs from the vascular plant (AtTPIs) and address their enzymatic modulation by redox agents. Cytoplasmic TPI (cTPI) and chloroplast TPI (pdTPI) share more than 60% amino acid identity and assemble as (β-α) dimers with high structural homology. cTPI and pdTPI harbor two and one accessible thiol groups per monomer respectively. cTPI and pdTPI present a cysteine at an equivalent structural position (C13 and C15 respectively) and cTPI also contains a specific solvent accessible cysteine at residue 218 (cTPI-C218). Site directed mutagenesis of residues pdTPI-C15, cTPI-C13, and cTPI-C218 to serine substantially decreases enzymatic activity, indicating that the structural integrity of these cysteines is necessary for catalysis. AtTPIs exhibit differential responses to oxidative agents, cTPI is susceptible to oxidative agents such as diamide and HO, whereas pdTPI is resistant to inhibition. Incubation of AtTPIs with the sulfhydryl conjugating reagents methylmethane thiosulfonate (MMTS) and glutathione inhibits enzymatic activity. However, the concentration necessary to inhibit pdTPI is at least two orders of magnitude higher than the concentration needed to inhibit cTPI. Western-blot analysis indicates that residues cTPI-C13, cTPI-C218, and pdTPI-C15 conjugate with glutathione. In summary, our data indicate that AtTPIs could be redox regulated by the derivatization of specific AtTPI cysteines (cTPI-C13 and pdTPI-C15 and cTPI-C218). Since AtTPIs have evolved by gene duplication, the higher resistance of pdTPI to redox agents may be an adaptive consequence to the redox environment in the chloroplast.

PubMed: 27999583
DOI: 10.3389/fpls.2016.01817

実験手法

X-RAY DIFFRACTION (1.6 Å)