Structural characterization of human Uch37 | Zendy

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

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Structural characterization of human Uch37

Author(s) -

Burgie Sethe E.,

Bingman Craig A.,

Soni Ameet B.,

Phillips George N.

Publication year - 2012

Publication title -

proteins: structure, function, and bioinformatics

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 1.699

H-Index - 191

eISSN - 1097-0134

pISSN - 0887-3585

DOI - 10.1002/prot.23147

Subject(s) - biology , ubiquitin , microbiology and biotechnology , deubiquitinating enzyme , proteasome , ubiquitin ligase , signal transduction , chromatin remodeling , biochemistry , histone , dna , gene

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.

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