Three-dimensional structure of the AAH26994.1 protein from Mus musculus, a putative eukaryotic Urm1.
We have used NMR spectroscopy to determine the solution structure of protein AAH26994.1 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 AAH26994.1 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 AAH26994.1 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 AAH26994.1). The structures of AAH26994.1 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.
Singh
Shanteri
S
Center for Eukaryotic Structural Genomics, Department of Biochemistry, University of Wisconsin-Madison, Madison, Wisconsin 53706-1544, USA.
Tonelli
Marco
M
Tyler
Robert C
RC
Bahrami
Arash
A
Lee
Min S
MS
Markley
John L
JL
D000595:Amino Acid Sequence; D000818:Animals; D051379:Mice; D008958:Models, Molecular; D008969:Molecular Sequence Data; D019906:Nuclear Magnetic Resonance, Biomolecular; D017510:Protein Folding; D017433:Protein Structure, Secondary; D013466:Sulfurtransferases / Q000737:chemistry; D025801:Ubiquitin / Q000737:chemistry; D014452:Ubiquitins / Q000737:chemistry*
D025801:Ubiquitin; D014452:Ubiquitins; C504904:Urm1 protein, mouse; D013466:Sulfurtransferases; C085585:molybdopterin synthase