Structure of ubiquitin-fold modifier 1-specific protease UfSP2

Byung Hak Ha, Young Joo Jeon, Sang Chul Shin, Kanako Tatsumi, Masaaki Komatsu, Keiji Tanaka, Christopher M. Watson, Gillian Wallis, Chin Ha Chung, Eunice EunKyeong Kim

    Research output: Contribution to journalArticlepeer-review

    Abstract

    Ubiquitin-fold modifier 1 (Ufm1)-specific protease 2 (UfSP2) is a cysteine protease that is responsible for the release of Ufm1 from Ufm1-conjugated cellular proteins, as well as for the generation of mature Ufm1 from its precursor. The 2.6 Å resolution crystal structure of mouse UfSP2 reveals that it is composed of two domains. The C-terminal catalytic domain is similar to UfSP1 with Cys294, Asp418, His420, Tyr 282, and a regulatory loop participating in catalysis. The novel N-terminal domain shows a unique structure and plays a role in the recognition of its cellular substrate C20orf116 and thus in the recruitment of UfSP2 to the endoplasmic reticulum, where C20orf116 predominantly localizes. Mutagenesis studies were carried out to provide the structural basis for understanding the loss of catalytic activity observed in a recently identified UfSP2 mutation that is associated with an autosomal dominant form of hip dysplasia. © 2011 by The American Society for Biochemistry and Molecular Biology, Inc.
    Original languageEnglish
    Pages (from-to)10248-10257
    Number of pages9
    JournalJournal of Biological Chemistry
    Volume286
    Issue number12
    DOIs
    Publication statusPublished - 25 Mar 2011

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