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

The proteasome-assembly chaperone Nas2 binds to the proteasome subunit Rpt5 using its PDZ domain. The structure of the Nas2 PDZ domain has been determined. The 26S proteasome is a 2.5 MDa protease dedicated to the degradation of ubiquitinated proteins in eukaryotes. The assembly of this complex cont...

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Bibliographic Details
Published inActa crystallographica. Section F, Structural biology communications Vol. 70; no. Pt 4
Main Authors Singh, Chingakham R., Lovell, Scott, Mehzabeen, Nurjahan, Chowdhury, Wasimul Q., Geanes, Eric S., Battaile, Kevin P., Roelofs, Jeroen
Format Journal Article
LanguageEnglish
Published United States 25.03.2014
Subjects
BASES
CONDENSED MATTER PHYSICS, SUPERCONDUCTIVITY AND SUPERFLUIDITY
FUNCTIONS
MATHEMATICAL METHODS AND COMPUTING
POLYPEPTIDES
RESOLUTION
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Summary:The proteasome-assembly chaperone Nas2 binds to the proteasome subunit Rpt5 using its PDZ domain. The structure of the Nas2 PDZ domain has been determined. 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.
ISSN:2053-230X
2053-230X
DOI:10.1107/S2053230X14003884