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PDBsum entry 5bxh
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Protein binding
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PDB id
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5bxh
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References listed in PDB file
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Key reference
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Title
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Structural insights into kctd protein assembly and cullin3 recognition.
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Authors
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A.X.Ji,
A.Chu,
T.K.Nielsen,
S.Benlekbir,
J.L.Rubinstein,
G.G.Privé.
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Ref.
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J Mol Biol, 2016,
428,
92.
[DOI no: ]
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PubMed id
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Abstract
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Cullin3 (Cul3)-based ubiquitin E3 ligase complexes catalyze the transfer of
ubiquitin from an E2 enzyme to target substrate proteins. In these assemblies,
the C-terminal region of Cul3 binds Rbx1/E2-ubiquitin, while the N-terminal
region interacts with various BTB (bric-à-brac, tramtrack, broad complex)
domain proteins that serve as substrate adaptors. Previous crystal structures of
the homodimeric BTB proteins KLHL3, KLHL11 and SPOP in complex with the
N-terminal domain of Cul3 revealed the features required for Cul3 recognition in
these proteins. A second class of BTB-domain-containing proteins, the KCTD
proteins, is also Cul3 substrate adaptors, but these do not share many of the
previously identified determinants for Cul3 binding. We report the pentameric
crystal structures of the KCTD1 and KCTD9 BTB domains and identify plasticity in
the KCTD1 rings. We find that the KCTD proteins 5, 6, 9 and 17 bind to Cul3 with
high affinity, while the KCTD proteins 1 and 16 do not have detectable binding.
Finally, we confirm the 5:5 assembly of KCTD9/Cul3 complexes by cryo-electron
microscopy and provide a molecular rationale for BTB-mediated Cul3 binding
specificity in the KCTD family.
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