Article
De novo design and evolution of artificial disulfide isomerase enzymes analogous to the bacterial DsbC.
The Journal of biological chemistry - 14 Nov 2008
Arredondo Silvia, Segatori Laura, Gilbert Hiram F, Georgiou George
Abstract excerpt
The Escherichia coli disulfide isomerase, DsbC is a V-shaped homodimer with each monomer comprising a dimerization region that forms part of a putative peptide-binding pocket and a thioredoxin catalytic domain. Disulfide isomerases from prokaryotes and eukaryotes exhibit little sequence homology but display very similar structural organization with two thioredoxin domains facing each other on top of the...
Topics
- Amino Acid Sequence
- Disulfides
- Escherichia coli
- Escherichia coli Proteins
- Membrane Proteins
- Models, Molecular
- Mutation
- Peptidylprolyl Isomerase
- Protein Binding
- Protein Disulfide-Isomerases
- Protein Engineering
- Protein Structure, Quaternary
- Protein Structure, Tertiary