1.15 Å resolution structure of the proteasome-assembly chaperone Nas2 PDZ domain

Chingakham R. Singh, Scott Lovell, Nurjahan Mehzabeen, Wasimul Q. Chowdhury, Eric S. Geanes, Kevin P. Battaile, Jeroen Roelofs

Research output: Contribution to journalArticlepeer-review

6 Scopus citations


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.

Original languageEnglish (US)
Pages (from-to)418-423
Number of pages6
JournalActa Crystallographica Section F:Structural Biology Communications
Issue number4
StatePublished - Apr 2014

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Genetics
  • Condensed Matter Physics


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