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PDBsum entry 2n9p
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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 and functional insights into the e3 ligase, Rnf126.
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Authors
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E.M.Krysztofinska,
S.Martínez-Lumbreras,
A.Thapaliya,
N.J.Evans,
S.High,
R.L.Isaacson.
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Ref.
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Sci Rep, 2016,
6,
26433.
[DOI no: ]
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PubMed id
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Abstract
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RNF126 is an E3 ubiquitin ligase that collaborates with the BAG6 sortase complex
to ubiquitinate hydrophobic substrates in the cytoplasm that are destined for
proteasomal recycling. Composed of a trimeric complex of BAG6, TRC35 and UBL4A
the BAG6 sortase is also associated with SGTA, a co-chaperone from which it can
obtain hydrophobic substrates. Here we solve the solution structure of the
RNF126 zinc finger domain in complex with the BAG6 UBL domain. We also
characterise an interaction between RNF126 and UBL4A and analyse the competition
between SGTA and RNF126 for the N-terminal BAG6 binding site. This work sheds
light on the sorting mechanism of the BAG6 complex and its accessory proteins
which, together, decide the fate of stray hydrophobic proteins in the aqueous
cytoplasm.
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