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 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 A 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.
Mizushima
Tsunehiro
T
Department of Biotechnology, Graduate School of Engineering, Nagoya University, Chikusa-ku, Nagoya 464-8603, Japan.
Tatsumi
Kanako
K
Ozaki
Yoko
Y
Kawakami
Tatsukuni
T
Suzuki
Atsuo
A
Ogasahara
Kyoko
K
Komatsu
Masaaki
M
Kominami
Eiki
E
Tanaka
Keiji
K
Yamane
Takashi
T
D000595:Amino Acid Sequence; D001665:Binding Sites; D003198:Computer Simulation; D003461:Crystallography; D008956:Models, Chemical; D008958:Models, Molecular; D008969:Molecular Sequence Data; D011485:Protein Binding; D011487:Protein Conformation; D011506:Proteins / Q000737:chemistry* / Q000648:ultrastructure*; D044763:Ubiquitin-Conjugating Enzymes / Q000737:chemistry* / Q000648:ultrastructure*