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PDBsum entry 5fer
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References listed in PDB file
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Key reference
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Title
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Functional role of trim e3 ligase oligomerization and regulation of catalytic activity.
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Authors
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M.G.Koliopoulos,
D.Esposito,
E.Christodoulou,
I.A.Taylor,
K.Rittinger.
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Ref.
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Embo J, 2016,
35,
1204-1218.
[DOI no: ]
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PubMed id
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Abstract
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TRIM E3 ubiquitin ligases regulate a wide variety of cellular processes and are
particularly important during innate immune signalling events. They are
characterized by a conserved tripartite motif in their N-terminal portion which
comprises a canonical RING domain, one or two B-box domains and a coiled-coil
region that mediates ligase dimerization. Self-association via the coiled-coil
has been suggested to be crucial for catalytic activity of TRIMs; however, the
precise molecular mechanism underlying this observation remains elusive. Here,
we provide a detailed characterization of the TRIM ligases TRIM25 and TRIM32 and
show how their oligomeric state is linked to catalytic activity. The crystal
structure of a complex between the TRIM25 RING domain and an ubiquitin-loaded E2
identifies the structural and mechanistic features that promote a closed E2~Ub
conformation to activate the thioester for ubiquitin transfer allowing us to
propose a model for the regulation of activity in the full-length protein. Our
data reveal an unexpected diversity in the self-association mechanism of TRIMs
that might be crucial for their biological function.
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