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PDBsum entry 1zu1
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RNA binding protein
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PDB id
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1zu1
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References listed in PDB file
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Key reference
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Title
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Solution structure of the n-Terminal zinc fingers of the xenopus laevis double-Stranded RNA-Binding protein zfa.
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Authors
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H.M.Möller,
M.A.Martinez-Yamout,
H.J.Dyson,
P.E.Wright.
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Ref.
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J Mol Biol, 2005,
351,
718-730.
[DOI no: ]
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PubMed id
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Abstract
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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.
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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.
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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.
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The above figures are
reprinted
by permission from Elsevier:
J Mol Biol
(2005,
351,
718-730)
copyright 2005.
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