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PDBsum entry 4y1h
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Signaling protein
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PDB id
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4y1h
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References listed in PDB file
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Key reference
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Title
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Assembly and structure of lys33-Linked polyubiquitin reveals distinct conformations.
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Authors
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Y.A.Kristariyanto,
S.Y.Choi,
S.A.Rehman,
M.S.Ritorto,
D.G.Campbell,
N.A.Morrice,
R.Toth,
Y.Kulathu.
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Ref.
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Biochem J, 2015,
467,
345-352.
[DOI no: ]
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PubMed id
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Abstract
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Ubiquitylation regulates a multitude of biological processes and this
versatility stems from the ability of ubiquitin (Ub) to form topologically
different polymers of eight different linkage types. Whereas some linkages have
been studied in detail, other linkage types including Lys33-linked polyUb are
poorly understood. In the present study, we identify an enzymatic system for the
large-scale assembly of Lys33 chains by combining the HECT (homologous to the
E6-AP C-terminus) E3 ligase AREL1 (apoptosis-resistant E3 Ub protein ligase 1)
with linkage selective deubiquitinases (DUBs). Moreover, this first
characterization of the chain selectivity of AREL1 indicates its preference for
assembling Lys33- and Lys11-linked Ub chains. Intriguingly, the crystal
structure of Lys33-linked diUb reveals that it adopts a compact conformation
very similar to that observed for Lys11-linked diUb. In contrast,
crystallographic analysis of Lys33-linked triUb reveals a more extended
conformation. These two distinct conformational states of Lys33-linked polyUb
may be selectively recognized by Ub-binding domains (UBD) and enzymes of the Ub
system. Importantly, our work provides a method to assemble Lys33-linked polyUb
that will allow further characterization of this atypical chain type.
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