 |
PDBsum entry 2lvo
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
Signaling protein/ligase
|
PDB id
|
|
|
|
2lvo
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
References listed in PDB file
|
|
|
Key reference
|
|
|
Title
|
|
Promiscuous interactions of gp78 e3 ligase cue domain with polyubiquitin chains.
|
|
|
Authors
|
|
S.Liu,
Y.Chen,
J.Li,
T.Huang,
S.Tarasov,
A.King,
A.M.Weissman,
R.A.Byrd,
R.Das.
|
|
|
Ref.
|
|
Structure, 2012,
20,
2138-2150.
|
|
|
PubMed id
|
|
|
|
|
|
Abstract
|
|
|
Recognition of ubiquitin and polyubiquitin chains by ubiquitin-binding domains
(UBDs) is vital for ubiquitin-mediated signaling pathways. The endoplasmic
reticulum resident RING finger ubiquitin ligase (E3) gp78 regulates critical
proteins via the ubiquitin-proteasome system to maintain cellular homeostasis
and includes a UBD known as the CUE domain, which is essential for function. A
probable role of this domain is to recognize ubiquitin-modified substrates,
enabling gp78 to assemble polyubiquitin chains on these substrates and mark them
for degradation. Here, we report the molecular details of the interaction of
gp78CUE domain with ubiquitin and diubiquitin. The gp78CUE domain exhibits a
well-defined set of interactions with ubiquitin and a dynamic, promiscuous
interaction with diubiquitin chains. This leads to a model in which the CUE
domain functions to both facilitate substrate binding and enable switching
between adjacent ubiquitin molecules of a growing chain to enable processivity
in ubiquitination.
|
|
|
|
|
|
|
