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Effects of a buried cysteine-to-serine mutation on yeast triosephosphate isomerase structure and stability.

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Hernández-Santoyo A, Domínguez-Ramírez L, Reyes-López CA, González-Mondragón E, Hernández-Arana A, Rodríguez-Romero A
OpenAccess logo Int J Mol Sci 13 10010-10021 (2012)
Cited: 7 times
EuropePMC logo PMID: 22949845

Abstract

All the members of the triosephosphate isomerase (TIM) family possess a cystein residue (Cys126) located near the catalytically essential Glu165. The evolutionarily conserved Cys126, however, does not seem to play a significant role in the catalytic activity. On the other hand, substitution of this residue by other amino acid residues destabilizes the dimeric enzyme, especially when Cys is replaced by Ser. In trying to assess the origin of this destabilization we have determined the crystal structure of Saccharomyces cerevisiae TIM (ScTIM) at 1.86 Å resolution in the presence of PGA, which is only bound to one subunit. Comparisons of the wild type and mutant structures reveal that a change in the orientation of the Ser hydroxyl group, with respect to the Cys sulfhydryl group, leads to penetration of water molecules and apparent destabilization of residues 132-138. The latter results were confirmed by means of Molecular Dynamics, which showed that this region, in the mutated enzyme, collapses at about 70 ns.

Articles - 4ff7 mentioned but not cited (2)

  1. PDB-Explorer: a web-based interactive map of the protein data bank in shape space. Jin X, Awale M, Zasso M, Kostro D, Patiny L, Reymond JL. BMC Bioinformatics 16 339 (2015)
  2. Effects of a buried cysteine-to-serine mutation on yeast triosephosphate isomerase structure and stability. Hernández-Santoyo A, Domínguez-Ramírez L, Reyes-López CA, González-Mondragón E, Hernández-Arana A, Rodríguez-Romero A. Int J Mol Sci 13 10010-10021 (2012)


Articles citing this publication (5)

  1. Cytosolic Triosephosphate Isomerase from Arabidopsis thaliana Is Reversibly Modified by Glutathione on Cysteines 127 and 218. Dumont S, Bykova NV, Pelletier G, Dorion S, Rivoal J. Front Plant Sci 7 1942 (2016)
  2. The role of site-directed point mutations in protein misfolding. Baruah A, Biswas P. Phys Chem Chem Phys 16 13964-13973 (2014)
  3. Mutation of a conserved tryptophan residue in the CBM3c of a GH9 endoglucanase inhibits activity. Kim SJ, Kim SH, Shin SK, Hyeon JE, Han SO. Int J Biol Macromol 92 159-166 (2016)
  4. Probing the role of highly conserved residues in triosephosphate isomerase--analysis of site specific mutants at positions 64 and 75 in the Plasmodial enzyme. Bandyopadhyay D, Murthy MR, Balaram H, Balaram P. FEBS J 282 3863-3882 (2015)
  5. 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, Fernández-de Gortari E, López-Castillo M, Baruch-Torres N, López-Hidalgo M, Peralta-Castro A, Díaz-Quezada C, Sotelo-Mundo RR, Benitez-Cardoza CG, Espinoza-Fonseca LM, Ochoa-Leyva A, Brieba LG. Front Mol Biosci 5 103 (2018)


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