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

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Issue Date
2014-04-01
Author
Singh, Chingakham Ranjit
Lovell, Scott
Mehzabeen, Nurjahan
Chowdhury, Wasimul Q.
Geanes, Eric S.
Battaile, Kevin P.
Roelofs, Jeroen
Publisher
Structural Biology Communications
Type
Article
Article Version
Scholarly/refereed, publisher version
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This is an open-access article distributed under the terms of the Creative Commons Attribution Licence, which permits unrestricted use, distribution, and reproduction in any medium, provided the original authors and source are cited.
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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.
URI
http://hdl.handle.net/1808/13617
DOI
https://doi.org/10.1107/S2053230X14003884
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Citation
Singh, C. R., Lovell, S., Mehzabeen, N., Chowdhury, W. Q., Geanes, E. S., Battaile, K. P. & Roelofs, J. (2014). 1.15 Å resolution structure of the proteasome-assembly chaperone Nas2 PDZ domain. Acta Cryst. F70, 418-423. http://dx.doi.org/10.1107/S2053230X14003884

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This is an open-access article distributed under the terms of the Creative Commons Attribution Licence, which permits unrestricted use, distribution, and reproduction in any medium, provided the original authors and source are cited.
Except where otherwise noted, this item's license is described as: This is an open-access article distributed under the terms of the Creative Commons Attribution Licence, which permits unrestricted use, distribution, and reproduction in any medium, provided the original authors and source are cited.