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1NSW

The Crystal Structure of the K18G Mutant of the thioredoxin from Alicyclobacillus acidocaldarius

Summary for 1NSW
Entry DOI10.2210/pdb1nsw/pdb
Related1NWL 1QUW 2TRX
DescriptorTHIOREDOXIN (2 entities in total)
Functional Keywordsthermostability, thioredoxin, electron transport
Biological sourceAlicyclobacillus acidocaldarius
Total number of polymer chains4
Total formula weight46052.65
Authors
Bartolucci, S.,De Simone, G.,Galdiero, S.,Improta, R.,Menchise, V.,Pedone, C.,Pedone, E.,Saviano, M. (deposition date: 2003-01-28, release date: 2003-08-05, Last modification date: 2024-10-30)
Primary citationBartolucci, S.,De Simone, G.,Galdiero, S.,Improta, R.,Menchise, V.,Pedone, C.,Pedone, E.,Saviano, M.
An integrated structural and computational study of the thermostability of two thioredoxin mutants from Alicyclobacillus acidocaldarius
J.Bacteriol., 185:4285-4289, 2003
Cited by
PubMed 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.
PubMed: 12837806
DOI: 10.1128/JB.185.14.4285-4289.2003
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.9 Å)
Structure validation

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