1WXS

Solution Structure of Ufm1, a ubiquitin-fold modifier

Summary for 1WXS

• Entry DOI: 10.2210/pdb1wxs/pdb
• Descriptor: Ubiquitin-fold Modifier 1 (1 entity in total)
• Functional Keywords: ubiquitin-fold, structural genomics, unknown function
• Biological source: Homo sapiens (human)
• Cellular location: Nucleus: P61960
• Total number of polymer chains: 1
• Total formula weight: 9540.01

Authors

Sasakawa, H.,Sakata, E.,Yamaguchi, Y.,Komatsu, M.,Tatsumi, K.,Kominami, E.,Tanaka, K.,Kato, K. (deposition date: 2005-02-01, release date: 2006-04-18, Last modification date: 2024-05-29)

Primary citation

Sasakawa, H.,Sakata, E.,Yamaguchi, Y.,Komatsu, M.,Tatsumi, K.,Kominami, E.,Tanaka, K.,Kato, K.
Solution structure and dynamics of Ufm1, a ubiquitin-fold modifier 1
Biochem.Biophys.Res.Commun., 343:21-26, 2006

PubMed Abstract: 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.

PubMed: 16527251
DOI: 10.1016/j.bbrc.2006.02.107

Experimental method

SOLUTION NMR