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PDBsum entry 1s4u
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Antiviral protein
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PDB id
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1s4u
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References listed in PDB file
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Key reference
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Title
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Crystal structure of ski8p, A wd-Repeat protein with dual roles in mRNA metabolism and meiotic recombination.
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Authors
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Z.Cheng,
Y.Liu,
C.Wang,
R.Parker,
H.Song.
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Ref.
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Protein Sci, 2004,
13,
2673-2684.
[DOI no: ]
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PubMed id
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Abstract
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Ski8p is a WD-repeat protein with an essential role for the Ski complex assembly
in an exosome-dependent 3'-to-5' mRNA decay. In addition, Ski8p is involved in
meiotic recombination by interacting with Spo11p protein. We have determined the
crystal structure of Ski8p from Saccharomyces cerevisiae at 2.2 A resolution.
The structure reveals that Ski8p folds into a seven-bladed beta propeller.
Mapping sequence conservation and hydrophobicities of amino acids on the
molecular surface of Ski8p reveals a prominent site on the top surface of the
beta propeller, which is most likely involved in mediating interactions of Ski8p
with Ski3p and Spo11p. Mutagenesis combined with yeast two-hybrid and GST
pull-down assays identified the top surface of the beta propeller as being
required for Ski8p binding to Ski3p and Spo11p. The functional implications for
Ski8p function in both mRNA decay and meiotic recombination are discussed.
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Figure 2.
Figure 2. Sequence alignment of S. cerevisiae Ski8, S.
macrospora Ski8, Schizosaccharmyces pombe Rec14, Homo sapiens
Rec14, and Mus musculus Rec14. The secondary structures of S.
cerevisiae Ski8 are shown. Invariant residues are white letters,
similar residues are red, and others are black. Residues
speculated for interactions with Ski3 and Spo11 are indicated by
*.
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Figure 4.
Figure 4. Molecular surface views of Ski8p. (A) Surface
representation of Ski8p showing the regions of high-to-low
sequence conservation shared by the eukaryotic Ski8 proteins,
corresponding to a color ramp from red to blue, respectively.
Invariant residues are labeled. The view is as in Figure 1A
Go- . (B)
Molecular surface of Ski8p colored according to residue
property, with hydrophobic residues green and other residues
gray. The hydrophobic residues are labeled. The view is as in A.
(C) The worm model showing the C  backbones of
Ski8p. Residues located either in hydrophobic patch or in
conserved patch are shown in stick models. The view is as in A.
A and B were produced using GRASP (Nicholls et al. 1991).
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The above figures are
reprinted
by permission from the Protein Society:
Protein Sci
(2004,
13,
2673-2684)
copyright 2004.
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