Structural characterization of human Uch37.

Burgie, E. Sethe; Bingman, Craig A.; Soni, Ameet B.; Phillips, George N.

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Structural characterization of human Uch37.

Published Date:

Sep 26 2011

Source:

Proteins. 80(2):649-654

Language:

English

[PDF-771.85 KB]

Details:

Personal Authors:

Burgie, E. Sethe ; Bingman, Craig A. ; Soni, Ameet B. ; Phillips, George N. ;

Keywords:

[+]

Pubmed ID:

21953935

Pubmed Central ID:

PMC3251636

Description:

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.

Document Type:

Journal Article

Collection(s):

CDC Public Access

Funding:

Supporting Files:

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