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Three-dimensional structure of the AAH26994.1 protein from Mus musculus, a putative eukaryotic Urm1

Center for Eukaryotic Structural Genomics, Department of Biochemistry, University of Wisconsin–Madison, Madison, Wisconsin 53706-1544, USA

(RECEIVED May 8, 2005; FINAL REVISION May 8, 2005; ACCEPTED May 11, 2005)

We have used NMR spectroscopy to determine the solution structure of protein AAH269941 from Mus musculus and propose that it represents the first three-dimensional structure of a ubiquitin-related modifier 1 (Urm1) protein. Amino acid sequence comparisons indicate that AAH269941 belongs to the Urm1 family of ubiquitin-like modifier proteins. The best characterized member of this family has been shown to be involved in nutrient sensing, invasive growth, and budding in yeast. Proteins in this family have only a weak sequence similarity to ubiquitin, and the structure of AAH269941 showed a much closer resemblance to MoaD subunits of molybdopterin synthases (known structures are of three bacterial MoaD proteins with 14%–26% sequence identity to AAH269941). The structures of AAH269941 and the MoaD proteins each contain the signature ubiquitin secondary structure fold, but all differ from ubiquitin largely in regions outside of this fold. This structural similarity bolsters the hypothesis that ubiquitin and ubiquitin-related proteins evolved from a protein-based sulfide donor system of the molybdopterin synthase type.

Keywords: Urm1; NMR spectroscopy; structural genomics; ubiquitin fold

Article and publication are at http://www.proteinscience.org/cgi/doi/10.1110/ps.051577605.

Reprint requests to: John L. Markley, Department of Biochemistry, University of Wisconsin–Madison, 433 Babcock Drive, Madison, WI 53706, USA; e-mail: markley{at}nmrfam.wisc.edu; fax: (608) 262-3179.

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