Int. J. Mol. Sci. 2012, 13(8), 10010-10021; doi:10.3390/ijms130810010
Article

Effects of a Buried Cysteine-To-Serine Mutation on Yeast Triosephosphate Isomerase Structure and Stability

1email, 2email, 3email, 4email, 5,* email and 1,* email
Received: 4 June 2012; in revised form: 24 July 2012 / Accepted: 26 July 2012 / Published: 10 August 2012
(This article belongs to the Special Issue Protein Crystallography in Molecular Biology)
This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
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.
Keywords: crystal structure; molecular dynamics; Saccharomyces cerevisiae; stability; triosephosphate isomerase
PDF Full-text Download PDF Full-Text [766 KB, uploaded 19 June 2014 04:24 CEST]

Export to BibTeX |
EndNote


MDPI and ACS Style

Hernández-Santoyo, A.; Domínguez-Ramírez, L.; Reyes-López, C.A.; González-Mondragón, E.; Hernández-Arana, A.; Rodríguez-Romero, A. Effects of a Buried Cysteine-To-Serine Mutation on Yeast Triosephosphate Isomerase Structure and Stability. Int. J. Mol. Sci. 2012, 13, 10010-10021.

AMA Style

Hernández-Santoyo A, Domínguez-Ramírez L, Reyes-López CA, González-Mondragón E, Hernández-Arana A, Rodríguez-Romero A. Effects of a Buried Cysteine-To-Serine Mutation on Yeast Triosephosphate Isomerase Structure and Stability. International Journal of Molecular Sciences. 2012; 13(8):10010-10021.

Chicago/Turabian Style

Hernández-Santoyo, Alejandra; Domínguez-Ramírez, Lenin; Reyes-López, César A.; González-Mondragón, Edith; Hernández-Arana, Andrés; Rodríguez-Romero, Adela. 2012. "Effects of a Buried Cysteine-To-Serine Mutation on Yeast Triosephosphate Isomerase Structure and Stability." Int. J. Mol. Sci. 13, no. 8: 10010-10021.

Int. J. Mol. Sci. EISSN 1422-0067 Published by MDPI AG, Basel, Switzerland RSS E-Mail Table of Contents Alert