1ZU1

Solution Structure of the N-terminal Zinc Fingers of the Xenopus laevis double stranded RNA binding protein ZFa

Summary for 1ZU1

• Entry DOI: 10.2210/pdb1zu1/pdb
• NMR Information: BMRB: 6655
• Descriptor: RNA binding protein ZFa, ZINC ION (2 entities in total)
• Functional Keywords: zinc finger protein, helix-loop-helix, helix-turn-helix, rna binding protein
• Biological source: Xenopus laevis (African clawed frog)
• Cellular location: Nucleus: Q8AVN9
• Total number of polymer chains: 1
• Total formula weight: 14202.73

Authors

Moller, H.M.,Martinez-Yamout, M.A.,Dyson, H.J.,Wright, P.E. (deposition date: 2005-05-29, release date: 2005-09-20, Last modification date: 2024-05-22)

Primary citation

Moller, H.M.,Martinez-Yamout, M.A.,Dyson, H.J.,Wright, P.E.
Solution structure of the N-terminal zinc fingers of the Xenopus laevis double-stranded RNA-binding protein ZFa
J.Mol.Biol., 351:718-730, 2005

PubMed Abstract: 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.

PubMed: 16051273
DOI: 10.1016/j.jmb.2005.06.032

Experimental method

SOLUTION NMR