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TitleLys63-linked ubiquitin chain adopts multiple conformational states for specific target recognition.
Journal, issue, pagesElife, Vol. 4, Year 2015
Publish dateJun 19, 2015
AuthorsZhu Liu / Zhou Gong / Wen-Xue Jiang / Ju Yang / Wen-Kai Zhu / Da-Chuan Guo / Wei-Ping Zhang / Mai-Li Liu / Chun Tang /
PubMed AbstractA polyubiquitin comprises multiple covalently linked ubiquitins and recognizes myriad targets. Free or bound to ligands, polyubiquitins are found in different arrangements of ubiquitin subunits. To ...A polyubiquitin comprises multiple covalently linked ubiquitins and recognizes myriad targets. Free or bound to ligands, polyubiquitins are found in different arrangements of ubiquitin subunits. To understand the structural basis for polyubiquitin quaternary plasticity and to explore the target recognition mechanism, we characterize the conformational space of Lys63-linked diubiquitin (K63-Ub2). Refining against inter-subunit paramagnetic NMR data, we show that free K63-Ub2 exists as a dynamic ensemble comprising multiple closed and open quaternary states. The quaternary dynamics enables K63-Ub2 to be specifically recognized in a variety of signaling pathways. When binding to a target protein, one of the preexisting quaternary states is selected and stabilized. A point mutation that shifts the equilibrium between the different states modulates the binding affinities towards K63-Ub2 ligands. This conformational selection mechanism at the quaternary level may be used by polyubiquitins of different lengths and linkages for target recognition.
External linksElife / PubMed:26090905 / PubMed Central
MethodsSAS (X-ray synchrotron) / NMR (solution)
Structure data

SASDCL6: Lys63-linked dimer ubiquitin (Polyubiquitin-C, ubiquitin)
Method: SAXS/SANS

PDB-2n2k:
Ensemble structure of the closed state of Lys63-linked diubiquitin in the absence of a ligand
Method: SOLUTION NMR

Chemicals

ChemComp-MTN:
S-[(1-oxyl-2,2,5,5-tetramethyl-2,5-dihydro-1H-pyrrol-3-yl)methyl] methanesulfonothioate

Source
  • homo sapiens (human)
KeywordsSIGNALING PROTEIN / polyubiquitin / ensemble structure / protein dynamics / ubiquitin signaling

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