An integrated structural and computational study of the thermostability of two thioredoxin mutants from Alicyclobacillus acidocaldarius.
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.
Bartolucci
Simonetta
S
Dipartimento di Chimica Biologica, University of Naples Federico II, Istituto di Biostrutture e Bioimmagini-CNR, 80134 Naples, Italy.
De Simone
Giuseppina
G
Galdiero
Stefania
S
Improta
Roberto
R
Menchise
Valeria
V
Pedone
Carlo
C
Pedone
Emilia
E
Saviano
Michele
M
D001407:Bacillus / Q000737:chemistry / Q000201:enzymology* / Q000235:genetics; D019295:Computational Biology / Q000379:methods*; D003460:Crystallization; D018360:Crystallography, X-Ray; D006358:Hot Temperature; D008958:Models, Molecular; D008969:Molecular Sequence Data; D009154:Mutation; D011487:Protein Conformation; D017510:Protein Folding; D013329:Structure-Activity Relationship; D013879:Thioredoxins / Q000737:chemistry* / Q000235:genetics* / Q000378:metabolism
D013879:Thioredoxins