Crystal structure of Ufc1, the Ufm1-conjugating enzyme

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...

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Bibliographic Details
Published in:Biochemical and biophysical research communications 2007-11, Vol.362 (4), p.1079-1084
Main Authors: Mizushima, Tsunehiro, Tatsumi, Kanako, Ozaki, Yoko, Kawakami, Tatsukuni, Suzuki, Atsuo, Ogasahara, Kyoko, Komatsu, Masaaki, Kominami, Eiki, Tanaka, Keiji, Yamane, Takashi
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Binding Sites
Computer Simulation
Crystal structure
Crystallography
Models, Chemical
Models, Molecular
Molecular Sequence Data
Protein Binding
Protein Conformation
Proteins - chemistry
Proteins - ultrastructure
Ubiquitin
Ubiquitin-Conjugating Enzymes - chemistry
Ubiquitin-Conjugating Enzymes - ultrastructure
Ufc1
Ufm1
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Summary: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.
ISSN:0006-291X
1090-2104
DOI:10.1016/j.bbrc.2007.08.129