Structural characterization of human Uch37.
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ABSTRACT:
SUBMITTER: Burgie SE
PROVIDER: S-EPMC3251636 | biostudies-literature | 2012 Feb
REPOSITORIES: biostudies-literature
Publications
Structural characterization of human Uch37.
Burgie Sethe E SE Bingman Craig A CA Soni Ameet B AB Phillips George N GN
Proteins 20110926 2
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 sta ...[more]
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