Crystal Structures of UbcH5b-Ubiquitin Intermediate and Cyclic Lys48-Linked Tetraubiquitin: Structural Insights into Polyubiquitin Chain Formation Mechanisms and its Dynamics

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  • SAKATA Eri
    Max-Planck-Institute of Biochemistry, Department of Molecular Structural Biology
  • SATOH Tadashi
    RIKEN Advanced Science Institute, Structural Glycobiology Team
  • YAMAGUCHI Yoshiki
    RIKEN Advanced Science Institute, Structural Glycobiology Team
  • WAKATSUKI Soichi
    Photon Factory, Institute of Materials Structure Science, KEK
  • KATO Koichi
    Okazaki Institute for Integrative Bioscience, Institute for Molecular Science, National Institute of Natural Sciences

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  • 細胞の中の不要なタンパク質に目印をつける仕組み
  • サイボウ ノ ナカ ノ フヨウ ナ タンパクシツ ニ メジルシ オ ツケル シクミ

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Abstract

Ubiquitination is one of the most versatile protein modifications, which regulates a variety of cellular events. Here we report the crystal structures of an intermediate of UbcH5b ∼ ubiquitin (Ub) conjugate and Lys48-linked cyclic tetraubiquitin. These structures provide structural insights into the mechanisms underlying formation and elongation of the ubiquitin chains.

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