Journal article
Crystal structures of Lys-63-linked tri- and di-ubiquitin reveal a highly extended chain architecture
Proteins, structure, function, and bioinformatics, v 77(4), pp 753-759
Dec 2009
PMID: 19731378
Featured in Collection : UN Sustainable Development Goals @ Drexel
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.
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Details
- Title
- Crystal structures of Lys-63-linked tri- and di-ubiquitin reveal a highly extended chain architecture
- Creators
- Stephen D Weeks - Department of Biochemistry and Molecular Biology, Drexel University College of Medicine, Philadelphia, Pennsylvania 19102, USAKimberly C GrastyLisa Hernandez-CuebasPatrick J Loll
- Publication Details
- Proteins, structure, function, and bioinformatics, v 77(4), pp 753-759
- Publisher
- Wiley; United States
- Grant note
- R01 NS065140 / NINDS NIH HHS Y01 GM000080 / NIGMS NIH HHS R21 NS048548 / NINDS NIH HHS R21 NS048548-02 / NINDS NIH HHS
- Resource Type
- Journal article
- Language
- English
- Academic Unit
- Biochemistry and Molecular Biology
- Web of Science ID
- WOS:000271602000001
- Scopus ID
- 2-s2.0-70450044394
- Other Identifier
- 991014877943604721
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InCites Highlights
Data related to this publication, from InCites Benchmarking & Analytics tool:
- Web of Science research areas
- Biochemistry & Molecular Biology
- Biophysics