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3NOB

Structure of K11-linked di-ubiquitin

Summary for 3NOB
Entry DOI10.2210/pdb3nob/pdb
DescriptorUbiquitin, SULFATE ION (3 entities in total)
Functional Keywordsubiquitin lysine-11, protein binding
Biological sourceHomo sapiens
Total number of polymer chains8
Total formula weight71088.89
Authors
Dong, K.C.,Matsumoto, M.L.,Hymowitz, S.G. (deposition date: 2010-06-25, release date: 2010-08-11, Last modification date: 2024-11-06)
Primary citationMatsumoto, M.L.,Wickliffe, K.E.,Dong, K.C.,Yu, C.,Bosanac, I.,Bustos, D.,Phu, L.,Kirkpatrick, D.S.,Hymowitz, S.G.,Rape, M.,Kelley, R.F.,Dixit, V.M.
K11-Linked Polyubiquitination in Cell Cycle Control Revealed by a K11 Linkage-Specific Antibody.
Mol.Cell, 39:477-484, 2010
Cited by
PubMed Abstract: Polyubiquitination is a posttranslational modification where ubiquitin chains containing isopeptide bonds linking one of seven ubiquitin lysines with the C terminus of an adjoining ubiquitin are covalently attached to proteins. While functions of K48- and K63-linked polyubiquitin are understood, the role(s) of noncanonical K11-linked chains is less clear. A crystal structure of K11-linked diubiquitin demonstrates a distinct conformation from K48- or K63-linked diubiquitin. We engineered a K11 linkage-specific antibody and use it to demonstrate that K11 chains are highly upregulated in mitotic human cells precisely when substrates of the ubiquitin ligase anaphase-promoting complex (APC/C) are degraded. These chains increased with proteasomal inhibition, suggesting they act as degradation signals in vivo. Inhibition of the APC/C strongly impeded the formation of K11-linked chains, suggesting that a single ubiquitin ligase is the major source of mitotic K11-linked chains. Our results underscore the importance of K11-linked ubiquitin chains as critical regulators of mitotic protein degradation.
PubMed: 20655260
DOI: 10.1016/j.molcel.2010.07.001
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.19 Å)
Structure validation

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