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Title: Crystal structures of Lys-63-linked tri- and di-ubiquitin reveal a highly extended chain architecture
Authors: Weeks, Stephen
Grasty, Kimberly C
Hernandez-Cuebas, Lisa
Loll, Patrick J # ×
Issue Date: Dec-2009
Publisher: John Wiley & Sons
Series Title: Proteins: Structure, Function and Genetics vol:77 issue:4 pages:753-759
Abstract: The covalent attachment of different types of poly-ubiquitin chains signal different outcomes for the proteins so targeted. For example, a protein modified with Lys-48-linked poly-ubiquitin chains is targeted for proteasomal degradation, whereas Lys-63-linked chains encode nondegradative signals. The structural features that enable these different types of chains to encode different signals have not yet been fully elucidated. We report here the X-ray crystal structures of Lys-63-linked tri- and di-ubiquitin at resolutions of 2.3 and 1.9 A, respectively. The tri- and di-ubiquitin species adopt essentially identical structures. In both instances, the ubiquitin chain assumes a highly extended conformation with a left-handed helical twist; the helical chain contains four ubiquitin monomers per turn and has a repeat length of approximately 110 A. Interestingly, Lys-48 ubiquitin chains also adopt a left-handed helical structure with a similar repeat length. However, the Lys-63 architecture is much more open than that of Lys-48 chains and exposes much more of the ubiquitin surface for potential recognition events. These new crystal structures are consistent with the results of solution studies of Lys-63 chain conformation, and reveal the structural basis for differential recognition of Lys-63 versus Lys-48 chains.
URI: 
ISSN: 0887-3585
Publication status: published
KU Leuven publication type: IT
Appears in Collections:Biocrystallography
× corresponding author
# (joint) last author

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