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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.
    View publication on PubMed

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 [2Fe–2S] 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
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