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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Published in | Acta crystallographica. Section F, Structural biology communications Vol. 70; no. Pt 4 |
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Main Authors | , , , , , , |
Format | Journal Article |
Language | English |
Published |
United States
25.03.2014
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Subjects | |
Online Access | Get full text |
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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. |
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ISSN: | 2053-230X 2053-230X |
DOI: | 10.1107/S2053230X14003884 |