Crystal structure of Ufc1, the Ufm1-conjugating enzyme

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• 作者：Tsunehiro Mizushima ; Kanako Tatsumi ; Yoko Ozaki ; Tatsukuni Kawakami ; Atsuo Suzuki ; Kyoko Ogasahara ; Masaaki Komatsu ; Eiki Kominami ; Keiji Tanaka ; Takashi Yamane
• 关键词：Ufm1 ; Ufc1 ; Crystal structure ; Ubiquitin ; E2
• 刊名：Biochemical and Biophysical Research Communications
• 出版年：2007
• 出版时间：3 November 2007
• 年：2007
• 卷：362
• 期：4
• 页码：1079-1084
• 全文大小：951 K

文摘

Ubiquitin and ubiquitin-like protein-conjugating enzymes play central roles in posttranslational modification processes. The ubiquitin-fold modifier 1 (Ufm1), one of a variety of ubiquitin-like modifiers, is covalently attached to target proteins via Uba5 and Ufm1-conjugating enzyme 1 (Ufc1), which are analogous to the E1 and E2 ubiquitylation enzymes. As Ufm1-related proteins are conserved in metazoa and plants, the Ufm1 system likely plays important roles in various multicellular organisms. Herein, we report the X-ray structure of human Ufc1 determined at 1.6 Å resolution. The Ufc1 structure comprises a canonical E2 domain and an additional N-terminal domain. The Uba5 binding site on Ufc1 was assigned by structural comparison of Ufc1 and Ubc12 and related mutational analyses. In addition, we show that the N-terminal unique domain of Ufc1 contributes to thermal stability.