PMID:22120742

Citation	Kagawa, W, Sagawa, T, Niki, H and Kurumizaka, H (2011) Structural basis for the DNA-binding activity of the bacterial β-propeller protein YncE. Acta Crystallogr. D Biol. Crystallogr. 67:1045-53
Abstract	β-Propellers are widely utilized in nature as recognition modules. The well conserved β-propeller fold exhibits a high degree of functional diversity, which is probably accomplished through variations in the surface properties of the proteins. Little is known about the interactions between β-propeller proteins and nucleic acids. In the present study, it has been found that the bacterial β-propeller protein YncE binds to DNA. Crystal structures of YncE in the free form and complexed with DNA revealed that the surface region of YncE corresponding to the `canonical' substrate-binding site forms essential contacts with DNA. A single DNA base within a single-stranded DNA region is trapped in the hydrophobic pocket located within the central channel of the β-propeller protein. These data provide physical evidence for the DNA-binding ability of the previously uncharacterized YncE and also suggest that the `canonical' substrate-binding site may be commonly adapted to facilitate nucleic acid binding in a subset of β-propeller proteins.
Links	PubMed Online version:10.1107/S0907444911045033
Keywords	Crystallography, X-Ray; DNA/chemistry; DNA/metabolism; Escherichia coli/chemistry; Escherichia coli/metabolism; Escherichia coli Proteins/chemistry; Escherichia coli Proteins/metabolism; Models, Molecular; Protein Structure, Tertiary; Structural Homology, Protein
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