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PDBsum entry 1pgu
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Protein binding
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PDB id
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1pgu
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Contents |
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* Residue conservation analysis
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References listed in PDB file
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Key reference
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Title
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The structure of aip1p, A wd repeat protein that regulates cofilin-Mediated actin depolymerization.
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Authors
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W.C.Voegtli,
A.Y.Madrona,
D.K.Wilson.
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Ref.
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J Biol Chem, 2003,
278,
34373-34379.
[DOI no: ]
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PubMed id
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Abstract
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Actin-interacting protein 1 (Aip1p) is a 67-kDa WD repeat protein known to
regulate the depolymerization of actin filaments by cofilin and is conserved in
organisms ranging from yeast to mammals. The crystal structure of Aip1p from
Saccharomyces cerevisiae was determined to a 2.3-A resolution and a final
crystallographic R-factor of 0.204. The structure reveals that the overall fold
is formed by two connected seven-bladed beta-propellers and has important
implications for the structure of Aip1 from other organisms and WD
repeat-containing proteins in general. These results were unexpected because a
maximum of 10 WD repeats had been reported in the literature for this protein
using sequence data. The surfaces of the beta-propellers formed by the D-A and
B-C loops are positioned adjacent to one another, giving Aip1p a shape that
resembles an open "clamshell." The mapping of conserved residues to
the structure of Aip1p reveals dense patches of conserved residues on the
surface of one beta-propeller and at the interface of the two beta-propellers.
These two patches of conserved residues suggest a potential binding site for
F-actin on Aip1p and that the orientation of the beta-propellers with respect to
one another plays a role in binding an actin-cofilin complex. In addition, the
conserved interface between the domains is mediated by a number of interactions
that appear to impart rigidity between the two domains of Aip1p and may make a
large substrate-induced conformational change difficult.
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Figure 2.
FIG. 2. Stereoview of 2F[o] - F[c] electron density map
contoured at 1.4  for residues 336-340,
350-354, and Trp-362 which confer rigidity at the  -propeller interface.
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Figure 3.
FIG. 3. Surface representations of Aip1p. A, Aip1p colored
according to electrostatic potential: red, -10 kT; white, 0 kT;
and blue, +10 kT. The molecule is in the same orientation as in
Fig. 1A. B, Aip1p colored according to sequence conservation as
defined under "Results." Regions of the molecular surface formed
by conserved residues are colored purple. Orientation is the
same as in A. C and D, Aip1p colored in the same manner as in A
and B, respectively. The molecule is rotated 180° on the y
axis relative to its orientation in A and B.
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The above figures are
reprinted
by permission from the ASBMB:
J Biol Chem
(2003,
278,
34373-34379)
copyright 2003.
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