Abstract
A great challenge to biologists is to create proteins with novel folds and tailored functions. As an alternative to de novo protein design, we investigated the structure of a randomly generated protein targeted to bind ATP. The crystal structure reveals a novel α/β fold bound to its ligand, representing both the first protein structure derived from in vitro evolution and the first nucleotide-binding protein stabilized by a zinc ion.
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Acknowledgements
We thank M.J. Bottomley for recording the NMR spectra and for useful discussions; C. Volpari and A. Vannini for help with in-house crystallography; M. Mertens and C. Rittmeyer, University of Frankfurt, for performing X-ray fluorescence (TXRF) analysis. P.L.S. was partially funded by Italian MIUR grant S053.
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Surdo, P., Walsh, M. & Sollazzo, M. A novel ADP- and zinc-binding fold from function-directed in vitro evolution. Nat Struct Mol Biol 11, 382–383 (2004). https://doi.org/10.1038/nsmb745
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DOI: https://doi.org/10.1038/nsmb745
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