PDBsum entry 1zu1

RNA binding protein

PDB id: 1zu1

Contents

Protein chain

127 a.a. *

Metals

_ZN ×2

* Residue conservation analysis

PDB id:

1zu1

Name:

RNA binding protein

Title:

Solution structure of the n-terminal zinc fingers of the xenopus laevis double stranded RNA binding protein zfa

Structure:

RNA binding protein zfa. Chain: a. Synonym: dsrbp-zfa. Engineered: yes

Source:

Xenopus laevis. African clawed frog. Organism_taxid: 8355. Expressed in: escherichia coli. Expression_system_taxid: 562.

NMR struc:

20 models

Authors:

H.M.Moller,M.A.Martinez-Yamout,H.J.Dyson,P.E.Wright

Key ref:

H.M.Möller et al. (2005). Solution structure of the N-terminal zinc fingers of the Xenopus laevis double-stranded RNA-binding protein ZFa. J Mol Biol, 351, 718-730. PubMed id: 16051273 DOI: 10.1016/j.jmb.2005.06.032

Date:

29-May-05 Release date: 20-Sep-05

Protein chain

Q8AVN9  (ZN346_XENLA) -  Zinc finger protein 346 from Xenopus laevis

Seq: 524 a.a.

Struc: 127 a.a.

Enzyme reactions

• Enzyme class: E.C.?

DOI no: 10.1016/j.jmb.2005.06.032

J Mol Biol 351:718-730 (2005)

PubMed id: 16051273

Solution structure of the N-terminal zinc fingers of the Xenopus laevis double-stranded RNA-binding protein ZFa.

H.M.Möller, M.A.Martinez-Yamout, H.J.Dyson, P.E.Wright.

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.

Selected figure(s)

Figure 4.
Figure 4. Heteronuclear 1H-15N NOEs measured for dsRBP-ZFa2-128. The cartoon on top of the Figure shows the location of secondary structure elements identified in the solution structure calculation.

Figure 7.
Figure 7. Superposition of (a) finger II of ZFa with finger 1 of TFIIIA (1tf3);35 (b) finger I of ZFa with finger 1 of SWI5 (1ncs);36 (c) finger II of ZFa with the first FOG zinc finger from U-shaped (1fv5);55 (d) finger 1 of ZFa with the U1C zinc finger (1uw2);38 (e) finger I of ZFa with the C-terminal domain of RecA (2reb).40 In each case, the ZFa finger structures are colored according to the scheme in Figure 5, and the superimposed structures are colored magenta.

The above figures are reprinted by permission from Elsevier: J Mol Biol (2005, 351, 718-730) copyright 2005.

Figures were selected by an automated process.