Crystallization (Comment) | Organism |
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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 | Comment | Organism |
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C73S | mutation improves protein stability. Decreasing order of stability is C73S/C85S, C73S, C85S, wild-type Pdx | Pseudomonas putida |
C73S/C85S | mutation improves protein stability. Decreasing order of stability is C73S/C85S, C73S, C85S, wild-type Pdx | Pseudomonas putida |
C85S | mutation improves protein stability. Decreasing order of stability is C73S/C85S, C73S, C85S, wild-type Pdx | Pseudomonas putida |
Organism | UniProt | Comment | Textmining |
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Pseudomonas putida | P16640 | - |
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