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A novel ADP- and zinc-binding fold from function-directed in vitro evolution.

Paola Lo Surdo·Martin A Walsh·Maurizio Sollazzo
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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 alpha/beta 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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Adenosine DiphosphateAdenosine TriphosphateCrystallography, X-RayDirected Molecular EvolutionProtein ConformationProtein FoldingProtein Structure, SecondaryProteinsRNA, MessengerZincJournal ArticleResearch Support, Non-U.S. Gov't

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Paola Lo Surdo, Martin A Walsh, Maurizio Sollazzo. 2004-03-14. A novel ADP- and zinc-binding fold from function-directed in vitro evolution.. https://doi.org/10.1038/nsmb745

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