title: Structural characterization of human Uch37.
abstract: Uch37 is a de-ubiquitylating enzyme that is functionally linked with the 26S proteasome via Rpn13, and is essential for metazoan development. Here, we report the X-ray crystal structure of full-length human Uch37 at 2.95 Å resolution. Uch37's catalytic domain is similar to those of all UCH enzymes characterized to date. The C-terminal extension is elongated, predominantly helical and contains coiled coil interactions. Additionally, we provide an initial characterization of Uch37's oligomeric state and identify a systematic error in previous analyses of Uch37 activity. Taken together, these data provide a strong foundation for further analysis of Uch37's several functions.
authors.affiliation: Department of Biochemistry, Center for Eukaryotic Structural Genomics, University of Wisconsin-Madison, Madison Wisconsin 53706-1544.
authors.forename: Sethe E
authors.initials: SE
authors.lastname: Burgie
authors.forename: Craig A
authors.initials: CA
authors.lastname: Bingman
authors.forename: Ameet B
authors.initials: AB
authors.lastname: Soni
authors.forename: George N
authors.initials: GN
authors.lastname: Phillips
mesh_terms: D001665:Binding Sites; D020134:Catalytic Domain; D018360:Crystallography, X-Ray; D047908:Intracellular Signaling Peptides and Proteins; D007700:Kinetics; D008562:Membrane Glycoproteins / Q000378:metabolism; D008958:Models, Molecular; D011487:Protein Conformation; D017434:Protein Structure, Tertiary; D043222:Ubiquitin Thiolesterase / Q000737:chemistry* / Q000378:metabolism
chemical_list: C500781:ADRM1 protein, human; D047908:Intracellular Signaling Peptides and Proteins; D008562:Membrane Glycoproteins; C421245:UCHL5 protein, human; D043222:Ubiquitin Thiolesterase