1uw1

A Novel ADP- and Zinc-binding fold from function-directed in vitro evolution

spinqualitylabelsall models 1uw1, resolution 1.94Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1uw1 is a 1 chain structure with sequence from Synthetic construct. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.94Å Ligands: ADP, ZN Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed 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. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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