Structural highlights
Publication Abstract from PubMed
beta-Propellers are widely utilized in nature as recognition modules. The well conserved beta-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 beta-propeller proteins and nucleic acids. In the present study, it has been found that the bacterial beta-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 beta-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 beta-propeller proteins.
Structural basis for the DNA-binding activity of the bacterial beta-propeller protein YncE.,Kagawa W, Sagawa T, Niki H, Kurumizaka H Acta Crystallogr D Biol Crystallogr. 2011 Dec;67(Pt 12):1045-53. Epub 2011, Nov 5. PMID:22120742[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Kagawa W, Sagawa T, Niki H, Kurumizaka H. Structural basis for the DNA-binding activity of the bacterial beta-propeller protein YncE. Acta Crystallogr D Biol Crystallogr. 2011 Dec;67(Pt 12):1045-53. Epub 2011, Nov 5. PMID:22120742 doi:10.1107/S0907444911045033
