1uw1

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Image:1uw1.jpg

1uw1, resolution 1.94Å

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A NOVEL ADP- AND ZINC-BINDING FOLD FROM FUNCTION-DIRECTED IN VITRO EVOLUTION

Overview

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.

About this Structure

1UW1 is a Single protein structure of sequence from [1] with and as ligands. Known structural/functional Site: . Full crystallographic information is available from OCA.

Reference

A novel ADP- and zinc-binding fold from function-directed in vitro evolution., Lo Surdo P, Walsh MA, Sollazzo M, Nat Struct Mol Biol. 2004 Apr;11(4):382-3. Epub 2004 Mar 14. PMID:15024384 [[Category: ]]

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