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PDBsum entry 1wr1
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Signaling protein
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PDB id
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1wr1
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References listed in PDB file
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Key reference
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Title
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Structure of the uba domain of dsk2p in complex with ubiquitin molecular determinants for ubiquitin recognition.
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Authors
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A.Ohno,
J.Jee,
K.Fujiwara,
T.Tenno,
N.Goda,
H.Tochio,
H.Kobayashi,
H.Hiroaki,
M.Shirakawa.
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Ref.
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Structure, 2005,
13,
521-532.
[DOI no: ]
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PubMed id
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Abstract
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The ubiquitin-associated (UBA) domain is one of the most frequently occurring
motifs that recognize ubiquitin tags. Dsk2p, a UBA-containing protein from
Saccharomyces cerevisiae, is involved in the ubiquitin-proteasome proteolytic
pathway and has been implicated in spindle pole duplication. Here we present the
solution structure of the UBA domain of Dsk2p (Dsk2(UBA)) in complex with
ubiquitin. The structure reveals that the UBA domain uses a mode of ubiquitin
recognition that is similar to that of the CUE domain, another ubiquitin binding
motif that shares low sequence homology but high structural similarity with UBA
domains. These two domains, as well as the structurally unrelated ubiquitin
binding motif UIM, provide a common, crucial recognition site for ubiquitin,
comprising a hydrogen-bonding acceptor for the amide group of Gly-47, and a
methyl group that packs against the hydrophobic pocket of ubiquitin formed by
Leu-8, Ile-44, His-68, and Val-70.
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Figure 4.
Figure 4. Comparison of UBA Domains
Ribbon diagrams
comparing the ubiquitin bound Dsk2^UBA (red) and two unliganded
UBA domains: the N-terminal UBA domain of hHR23A^UBA1 (PDB code
1IFY; orange) and the UBA domain of rat p47^UBA (PDB code 1V92;
pink). The side chains of conserved residues, which are
important for formation of the hydrophobic core and structural
integrity, are indicated in yellow. These residues correspond to
those shown in yellow font in Figure 1.
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The above figure is
reprinted
by permission from Cell Press:
Structure
(2005,
13,
521-532)
copyright 2005.
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