Structural characterization of human Uch37

✍ Scribed by Sethe E. Burgie; Craig A. Bingman; Ameet B. Soni; George N. Phillips Jr.

• Book ID: 105358310
• Publisher: John Wiley and Sons
• Year: 2011
• Tongue: English
• Weight: 333 KB
• Volume: 80
• Category: Article
• ISSN: 0887-3585
• DOI: 10.1002/prot.23147

✦ Synopsis

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.