6bve

From Proteopedia

Triosephosphate isomerase of Synechocystis in complex with 2-Phosphoglycolic acid

PDB ID 6bve

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Structural highlights

6bve is a 2 chain structure with sequence from Synechocystis sp. PCC 6803 substr. Kazusa. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 1.78Å
Ligands:	,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

TPIS_SYNY3 Involved in the gluconeogenesis. Catalyzes stereospecifically the conversion of dihydroxyacetone phosphate (DHAP) to D-glyceraldehyde-3-phosphate (G3P).

Publication Abstract from PubMed

In plants, the ancestral cyanobacterial triosephosphate isomerase (TPI) was replaced by a duplicated version of the cytosolic TPI. This isoform acquired a transit peptide for chloroplast localization and functions in the Calvin-Benson cycle. To gain insight into the reasons for this gene replacement in plants, we characterized the TPI from the photosynthetic bacteria Synechocystis (SyTPI). SyTPI presents typical TPI enzyme kinetics profiles and assembles as a homodimer composed of two subunits that arrange in a (beta-alpha)8 fold. We found that oxidizing agents diamide (DA) and H2O2, as well as thiol-conjugating agents such as oxidized glutathione (GSSG) and methyl methanethiosulfonate (MMTS), do not inhibit the catalytic activity of SyTPI at concentrations required to inactivate plastidic and cytosolic TPIs from the plant model Arabidopsis thaliana (AtpdTPI and AtcTPI, respectively). The crystal structure of SyTPI revealed that each monomer contains three cysteines, C47, C127, and C176; however only the thiol group of C176 is solvent exposed. While AtcTPI and AtpdTPI are redox-regulated by chemical modifications of their accessible and reactive cysteines, we found that C176 of SyTPI is not sensitive to redox modification in vitro. Our data let us postulate that SyTPI was replaced by a eukaryotic TPI, because the latter contains redox-sensitive cysteines that may be subject to post-translational modifications required for modulating TPI's enzymatic activity.

Structural Basis for the Limited Response to Oxidative and Thiol-Conjugating Agents by Triosephosphate Isomerase From the Photosynthetic Bacteria Synechocystis.,Castro-Torres E, Jimenez-Sandoval P, Fernandez-de Gortari E, Lopez-Castillo M, Baruch-Torres N, Lopez-Hidalgo M, Peralta-Castro A, Diaz-Quezada C, Sotelo-Mundo RR, Benitez-Cardoza CG, Espinoza-Fonseca LM, Ochoa-Leyva A, Brieba LG Front Mol Biosci. 2018 Nov 27;5:103. doi: 10.3389/fmolb.2018.00103. eCollection, 2018. PMID:30538993^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Castro-Torres E, Jimenez-Sandoval P, Fernandez-de Gortari E, Lopez-Castillo M, Baruch-Torres N, Lopez-Hidalgo M, Peralta-Castro A, Diaz-Quezada C, Sotelo-Mundo RR, Benitez-Cardoza CG, Espinoza-Fonseca LM, Ochoa-Leyva A, Brieba LG. Structural Basis for the Limited Response to Oxidative and Thiol-Conjugating Agents by Triosephosphate Isomerase From the Photosynthetic Bacteria Synechocystis. Front Mol Biosci. 2018 Nov 27;5:103. doi: 10.3389/fmolb.2018.00103. eCollection, 2018. PMID:30538993 doi:http://dx.doi.org/10.3389/fmolb.2018.00103