1zu1
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Solution Structure of the N-terminal Zinc Fingers of the Xenopus laevis double stranded RNA binding protein ZFa
OverviewOverview
Several zinc finger proteins have been discovered recently that bind, specifically to double-stranded RNA. These include the mammalian JAZ and, wig proteins, and the seven-zinc finger protein ZFa from Xenopus laevis., We have determined the solution structure of a 127 residue fragment of, ZFa, which consists of two zinc finger domains connected by a linker that, remains unstructured in the free protein in solution. The first zinc, finger consists of a three-stranded beta-sheet and three helices, while, the second finger contains only a two-stranded sheet and two helices. The, common structures of the core regions of the two fingers are, superimposable. Each finger has a highly electropositive surface that maps, to a helix-kink-helix motif. There is no evidence for interactions between, the two fingers, consistent with the length (24 residues) and unstructured, nature of the intervening linker. Comparison with a number of other, proteins shows similarities in the topology and arrangement of secondary, structure elements with canonical DNA-binding zinc fingers, with protein, interaction motifs such as FOG zinc fingers, and with other DNA-binding, and RNA-binding proteins that do not contain zinc. However, in none of, these cases does the alignment of these structures with the ZFa zinc, fingers produce a consistent picture of a plausible RNA-binding interface., We conclude that the ZFa zinc fingers represent a new motif for the, binding of double-stranded RNA.
About this StructureAbout this Structure
1ZU1 is a Single protein structure of sequence from Xenopus laevis with as ligand. Full crystallographic information is available from OCA.
ReferenceReference
Solution structure of the N-terminal zinc fingers of the Xenopus laevis double-stranded RNA-binding protein ZFa., Moller HM, Martinez-Yamout MA, Dyson HJ, Wright PE, J Mol Biol. 2005 Aug 26;351(4):718-30. PMID:16051273
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