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Proteins. 2012 Feb;80(2):649-54. doi: 10.1002/prot.23147. Epub 2011 Sep 26.

Structural characterization of human Uch37.

Author information

1
Department of Biochemistry, Center for Eukaryotic Structural Genomics, University of Wisconsin-Madison, Madison Wisconsin 53706-1544.

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.

KEYWORDS:

UCH-L5; deubiquitylating enzymes; proteasome; protein assembly; ubiquitin; ubiquitin C-terminal hydrolase

PMID:
21953935
PMCID:
PMC3251636
DOI:
10.1002/prot.23147
[Indexed for MEDLINE]
Free PMC Article

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