Literature summary extracted from
Sevrioukova, I.; Garcia, C.; Li, H.; Bhaskar, B.; Poulos, T.
Crystal structure of putidaredoxin, the [2Fe-2S] component of the P450cam monooxygenase system from Pseudomonas putida (2003), J. Mol. Biol., 333, 377-392.
Crystallization (Commentary)
EC Number |
Crystallization (Comment) |
Organism |
---|
1.18.1.5 |
crystal structures of C73S/C85S and C73S mutants, to 1.47 A and 1.65 A resolution, respectively, are nearly identical and very similar to those of bovine adrenodoxin and Escherichia coli ferredoxin. In particular, formation of a hydrogen bond between the side-chain of Y51 and the carbonyl oxygen atom of E77 and the presence of two well-ordered water molecules linking the interaction domain and the C-terminal peptide to the core of the molecule are unique to Pdx. The folding topology of the NMR model is similar to that of the X-ray structure of Pdx. W106, important in the Pdr-to-Pdx and Pdx-to-P450cam electron transfer reactions, is in a position to regulate and/or mediate electron transfer to or from the [2Fe2S] center of Pdx |
Pseudomonas putida |
Protein Variants
EC Number |
Protein Variants |
Comment |
Organism |
---|
1.18.1.5 |
C73S |
mutation improves protein stability. Decreasing order of stability is C73S/C85S, C73S, C85S, wild-type Pdx |
Pseudomonas putida |
1.18.1.5 |
C73S/C85S |
mutation improves protein stability. Decreasing order of stability is C73S/C85S, C73S, C85S, wild-type Pdx |
Pseudomonas putida |
1.18.1.5 |
C85S |
mutation improves protein stability. Decreasing order of stability is C73S/C85S, C73S, C85S, wild-type Pdx |
Pseudomonas putida |
Organism
EC Number |
Organism |
UniProt |
Comment |
Textmining |
---|
1.18.1.5 |
Pseudomonas putida |
P16640 |
- |
- |