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Published March 24, 1999 | Published
Journal Article Open

Rubredoxin Variant Folds without Iron


Pyroccocus furiosus rubredoxin (PFRD), like most studied hyperthermophilic proteins, does not undergo reversible folding. The irreversibility of folding is thought to involve PFRD's iron-binding site. Here we report a PFRD variant (PFRD-XC4) whose iron binding site was redesigned to eliminate iron binding using a computational design algorithm. PFRD-XC4 folds without iron and exhibits reversible folding with a melting temperature of 82 °C, a thermodynamic stability of 3.2 kcal mol^(-1) at 1 °C, and NMR chemical shifts similar to that of the wild-type protein. This variant should provide a tractable model system for studying the thermodynamic origins of protein hyperthermostability.

Additional Information

© 1999 American Chemical Society. Received October 1, 1998. Publication Date (Web): March 5, 1999. We thank M. K. Eidness for the wild type Pyroccocus furiosus rubredoxin gene used in this study, S. M. Malakauskas, S. Ross, and C. Sarisky for technical assistance and discussions, and B. I. Dahiyat for discussions. The work was supported by the Howard Hughes Medical Institute (S.L.M.) and a NIH training grant (P.S.).

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Published - Strop_1999_J_Am_Chem_Soc_Rubredoxin_variant_folds_without_iron.pdf


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