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PDBsum entry 4zpz
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Signaling protein
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PDB id
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4zpz
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References listed in PDB file
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Key reference
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Title
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A versatile strategy for the semisynthetic production of ser65 phosphorylated ubiquitin and its biochemical and structural characterisation.
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Authors
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C.Han,
K.C.Pao,
A.Kazlauskaite,
M.M.Muqit,
S.Virdee.
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Ref.
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Chembiochem, 2015,
16,
1574-1579.
[DOI no: ]
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PubMed id
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Abstract
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Ubiquitin phosphorylation is emerging as an important regulatory layer in the
ubiquitin system. This is exemplified by the phosphorylation of ubiquitin on
Ser65 by the Parkinson's disease-associated kinase PINK1, which mediates the
activation of the E3 ligase Parkin. Additional phosphorylation sites on
ubiquitin might also have important cellular roles. Here we report a versatile
strategy for preparing phosphorylated ubiquitin. We biochemically and
structurally characterise semisynthetic phospho-Ser65-ubiquitin. Unexpectedly,
we observed disulfide bond formation between ubiquitin molecules, and hence a
novel crystal form. The method outlined provides a direct approach to study the
combinatorial effects of phosphorylation on ubiquitin function. Our analysis
also suggests that disulfide engineering of ubiquitin could be a useful strategy
for obtaining alternative crystal forms of ubiquitin species thereby
facilitating structural validation.
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