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

Simonetta Bartolucci; Giuseppina De Simone; Stefania Galdiero; Roberto Improta; Valeria Menchise; Carlo Pedone; Emilia Pedone; Michele Saviano

doi:10.1128/JB.185.14.4285-4289.2003

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.

Authors

Simonetta Bartolucci¹, Giuseppina De Simone, Stefania Galdiero, Roberto Improta, Valeria Menchise, Carlo Pedone, Emilia Pedone, Michele Saviano

Affiliation

¹ Dipartimento di Chimica Biologica, University of Naples Federico II, Istituto di Biostrutture e Bioimmagini-CNR, 80134 Naples, Italy.

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