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- Title
1.15 Å resolution structure of the proteasome-assembly chaperone Nas2 PDZ domain.
- Authors
Singh, Chingakham R.; Lovell, Scott; Mehzabeen, Nurjahan; Chowdhury, Wasimul Q.; Geanes, Eric S.; Battaile, Kevin P.; Roelofs, Jeroen
- Abstract
The 26S proteasome is a 2.5 MDa protease dedicated to the degradation of ubiquitinated proteins in eukaryotes. The assembly of this complex containing 66 polypeptides is assisted by at least nine proteasome-specific chaperones. One of these, Nas2, binds to the proteasomal AAA-ATPase subunit Rpt5. The PDZ domain of Nas2 binds to the C-terminal tail of Rpt5; however, it does not require the C-terminus of Rpt5 for binding. Here, the 1.15 Å resolution structure of the PDZ domain of Nas2 is reported. This structure will provide a basis for further insights regarding the structure and function of Nas2 in proteasome assembly.
- Subjects
PROTEASOMES; MOLECULAR chaperones; PROTEOLYTIC enzymes; EUKARYOTES; POLYPEPTIDES
- Publication
Acta Crystallographica: Section F, Structural Biology Communications, 2014, Vol 70, Issue 4, p418
- ISSN
2053-230X
- Publication type
Article
- DOI
10.1107/S2053230X14003884