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spinqualitylabelsall models 2z6o, resolution 1.60Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

Crystal Structure of the Ufc1, Ufm1 conjugating enzyme 1

Overview

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 1.6A 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.

About this Structure

2Z6O is a Single protein structure of sequence from Homo sapiens with as ligand. Active as Ubiquitin--protein ligase, with EC number 6.3.2.19 Full crystallographic information is available from OCA.

Reference

Crystal structure of Ufc1, the Ufm1-conjugating enzyme., Mizushima T, Tatsumi K, Ozaki Y, Kawakami T, Suzuki A, Ogasahara K, Komatsu M, Kominami E, Tanaka K, Yamane T, Biochem Biophys Res Commun. 2007 Nov 3;362(4):1079-84. Epub 2007 Aug 30. PMID:17825256

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