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PDBsum entry 1wrd
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Protein transport/signaling protein
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PDB id
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1wrd
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References listed in PDB file
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Key reference
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Title
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Structural basis for recognition of ubiquitinated cargo by tom1-Gat domain.
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Authors
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M.Akutsu,
M.Kawasaki,
Y.Katoh,
T.Shiba,
Y.Yamaguchi,
R.Kato,
K.Kato,
K.Nakayama,
S.Wakatsuki.
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Ref.
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FEBS Lett, 2005,
579,
5385-5391.
[DOI no: ]
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PubMed id
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Abstract
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Tom1 (Target of Myb1) is suggested to be involved in the transport of
ubiquitinated proteins, through the interaction of its GAT (GGA and Tom1) domain
with ubiquitin. Here, we demonstrate that the three-helix bundle of Tom1-GAT has
two ubiquitin-binding sites recognizing the hydrophobic Ile44 surface of
ubiquitin. The complex crystal structure demonstrates that the first site is a
hydrophobic patch on helices alpha1 and alpha2. NMR and biochemical data
revealed that the N-terminal half of helix alpha3 of Tom1-GAT constitutes the
second, stronger binding site. The double-sided ubiquitin binding enhances the
efficiency of recognition of ubiquitinated proteins by Tom1.
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Figure 1.
Fig. 1. (A) Crystal structure of Tom1-GAT/ubiquitin
complex, and (B) a view rotated by 90° about the horizontal
axis. (C) Superposition of Tom1-GAT molecule (red), GGA1-GAT
(blue) and GGA3-GAT (cyan), in the same view as (A).
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Figure 3.
Fig. 3. Ubiquitin-binding Site 1 of Tom1-GAT. (A) Stereo
ribbon representation of the interface between Site 1 of
Tom1-GAT (red) and ubiquitin (blue), in the same view as Fig.
1A. Side chains of Tom1-GAT and ubiquitin directly involved in
the interactions are shown in ball-and-stick models with labels.
The salt bridge between Glu256 and Arg42 is indicated by a red
line. (B) The molecular surface of ubiquitin is shown with a
ribbon drawing of GAT, in the same view as (A). Hydrophobic
residues of ubiquitin are colored green. Residues participating
in the interaction are labeled. (C) The molecular surface of GAT
is shown with a line drawing of ubiquitin, in the view rotated
180° about the vertical axis relative to (A).
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The above figures are
reprinted
by permission from the Federation of European Biochemical Societies:
FEBS Lett
(2005,
579,
5385-5391)
copyright 2005.
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