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1wxs
From Proteopedia
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[[Image:1wxs.gif|left|200px]] | [[Image:1wxs.gif|left|200px]] | ||
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'''Solution Structure of Ufm1, a ubiquitin-fold modifier''' | '''Solution Structure of Ufm1, a ubiquitin-fold modifier''' | ||
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[[Category: Tatsumi, K.]] | [[Category: Tatsumi, K.]] | ||
[[Category: Yamaguchi, Y.]] | [[Category: Yamaguchi, Y.]] | ||
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Revision as of 11:16, 3 May 2008
Solution Structure of Ufm1, a ubiquitin-fold modifier
Overview
The ubiquitin-fold modifier 1 (Ufm1) is one of various ubiquitin-like modifiers and conjugates to target proteins in cells through Uba5 (E1) and Ufc1 (E2). The Ufm1-system is conserved in metazoa and plants, suggesting its potential roles in various multicellular organisms. Herein, we analyzed the solution structure and dynamics of human Ufm1 (hsUfm1) by nuclear magnetic resonance spectroscopy. Although the global fold of hsUfm1 is similar to those of ubiquitin (Ub) and NEDD8, the cluster of acidic residues conserved in Ub and NEDD8 does not exist on the Ufm1 surface. 15N spin relaxation data revealed that the amino acid residues of hsUfm1 exhibiting conformational fluctuations form a cluster at the C-terminal segment and its spatial proximity, which correspond to the versatile ligand-binding sites of Ub and other ubiquitin-like proteins (Ubls). We suggest that Ub and other Ubl-modifiers share a common feature of potential conformational multiplicity, which might be associated with the broad ligand specificities of these proteins.
About this Structure
1WXS is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Solution structure and dynamics of Ufm1, a ubiquitin-fold modifier 1., Sasakawa H, Sakata E, Yamaguchi Y, Komatsu M, Tatsumi K, Kominami E, Tanaka K, Kato K, Biochem Biophys Res Commun. 2006 Apr 28;343(1):21-6. Epub 2006 Feb 28. PMID:16527251 Page seeded by OCA on Sat May 3 14:16:49 2008
