Calculation of Cys 30 ΔpKa's and oxidising power for DsbA mutants

Calculation of Cys 30 ΔpKa's and oxidising power for DsbA mutants

DsbA possesses a redox active disulphide, with the equilibrium strongly shifted towards the reduced form as compared to its structural homologue, thioredoxin. It is widely believed that the two amino acids that separate the active site cysteines play a crucial role in determining oxidising power wit...

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Veröffentlicht in:FEBS letters 1996-04, Vol.385 (1-2), p.105-108
Hauptverfasser: Warwicker, J., Gane, P.J.
Format: Artikel
Sprache:eng
Schlagworte:
Binding Sites
Computer Simulation
Cysteine - chemistry
Disulphide bridge
Electrophysiology
Electrostatic interaction
Escherichia coli - enzymology
Isomerases - chemistry
Isomerases - genetics
Isomerases - metabolism
Kinetics
Molecular modelling
Mutation
Oxidation-Reduction
Protein Conformation
Protein Disulfide-Isomerases
Redox potential
Thioredoxin
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Beschreibung
Zusammenfassung:DsbA possesses a redox active disulphide, with the equilibrium strongly shifted towards the reduced form as compared to its structural homologue, thioredoxin. It is widely believed that the two amino acids that separate the active site cysteines play a crucial role in determining oxidising power within the thioredoxin family. Data concerning redox and pKa properties for DsbA mutants in this region are available. Electrostatics calculations show reasonable agreement with the experimental data, and support the suggestion that amino acids outside of the CXXC active site sequence are as important in determining oxidising power within the thioredoxin family as are those within it.
ISSN:0014-5793
1873-3468
DOI:10.1016/0014-5793(96)00358-4