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PDBsum entry 2g45
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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 ubiquitin binding domain znf ubp recognizes the c-Terminal diglycine motif of unanchored ubiquitin.
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Authors
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F.E.Reyes-Turcu,
J.R.Horton,
J.E.Mullally,
A.Heroux,
X.Cheng,
K.D.Wilkinson.
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Ref.
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Cell, 2006,
124,
1197-1208.
[DOI no: ]
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PubMed id
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Abstract
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Ubiquitin binding proteins regulate the stability, function, and/or localization
of ubiquitinated proteins. Here we report the crystal structures of the
zinc-finger ubiquitin binding domain (ZnF UBP) from the deubiquitinating enzyme
isopeptidase T (IsoT, or USP5) alone and in complex with ubiquitin. Unlike other
ubiquitin binding domains, this domain contains a deep binding pocket where the
C-terminal diglycine motif of ubiquitin is inserted, thus explaining the
specificity of IsoT for an unmodified C terminus on the proximal subunit of
polyubiquitin. Mutations in the domain demonstrate that it is required for
optimal catalytic activation of IsoT. This domain is present in several other
protein families, and the ZnF UBP domain from an E3 ligase also requires the C
terminus of ubiquitin for binding. These data suggest that binding the ubiquitin
C terminus may be necessary for the function of other proteins.
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Figure 3.
Figure 3. Structure of IsoT ZnF UBP Domain Bound to
Ubiquitin
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Figure 4.
Figure 4. Interaction between Conserved Residues of the ZnF
UBP Domain of IsoT and Ubiquitin
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The above figures are
reprinted
by permission from Cell Press:
Cell
(2006,
124,
1197-1208)
copyright 2006.
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