An integrated structural and computational study of the thermostability of two thioredoxin mutants from Alicyclobacillus acidocaldarius

J Bacteriol. 2003 Jul;185(14):4285-9. doi: 10.1128/JB.185.14.4285-4289.2003.

Abstract

We report a crystallographic and computational analysis of two mutant forms of the Alicyclobacillus acidocaldarius thioredoxin (BacTrx) done in order to evaluate the contribution of two specific amino acids to the thermostability of BacTrx. Our results suggest that the thermostability of BacTrx may be modulated by mutations affecting the overall electrostatic energy of the protein.

MeSH terms

  • Bacillus / chemistry
  • Bacillus / enzymology*
  • Bacillus / genetics
  • Computational Biology / methods*
  • Crystallization
  • Crystallography, X-Ray
  • Hot Temperature*
  • Models, Molecular
  • Molecular Sequence Data
  • Mutation*
  • Protein Conformation
  • Protein Folding
  • Structure-Activity Relationship
  • Thioredoxins / chemistry*
  • Thioredoxins / genetics*
  • Thioredoxins / metabolism

Substances

  • Thioredoxins

Associated data

  • PDB/1NSW
  • PDB/1NW2