Crystal structures of Lys-63-linked tri- and di-ubiquitin reveal a highly extended chain architecture.
Crystal structures of Lys-63-linked tri- and di-ubiquitin reveal a highly extended chain architecture.
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DOI：
10.1002/prot.22568
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发表时间：
2009-12
影响因子：
2.9
通讯作者：
Loll, Patrick J.
中科院分区：
文献类型：
--
作者：
Weeks, Stephen D.;Grasty, Kimberly C.;Hernandez-Cuebas, Lisa;Loll, Patrick J.
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 non-degradative 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 Å, 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 Å. 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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DOI：
10.1107/s0907444904019158
发表时间：
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影响因子：
2.2
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