Article
Three-dimensional structure of lipoamide dehydrogenase from Pseudomonas fluorescens at 2.8 A resolution. Analysis of redox and thermostability properties.
Journal of molecular biology - 20 Apr 1993
Mattevi A, Obmolova G, Kalk K H, van Berkel W J, Hol W G
Abstract excerpt
The structure of Pseudomonas fluorescens lipoamide dehydrogenase, a dimeric flavoenzyme with a molecular mass of 106,000 daltons, was solved by the molecular replacement method and refined to an R-factor of 19.4% at 2.8 A resolution. The root-mean-square difference from ideal values for bonds and...
Topics
- Amino Acid Sequence
- Azotobacter vinelandii
- Binding Sites
- Catalysis
- Crystallization
- Dihydrolipoamide Dehydrogenase
- Electronic Data Processing
- Flavin-Adenine Dinucleotide
- Hydrogen Bonding
- Models, Molecular
- Molecular Sequence Data
- Mutation
- NAD
- Oxidation-Reduction
- Protein Conformation
- Protein Denaturation
- Pseudomonas fluorescens
- Recombinant Proteins