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1.15 Å resolution structure of the proteasome-assembly chaperone Nas2 PDZ domain
Singh, Chingakham Ranjit Lovell, Scott Mehzabeen, Nurjahan Chowdhury, Wasimul Q. Geanes, Eric S. Battaile, Kevin P. Roelofs, Jeroen
Singh, Chingakham Ranjit
Lovell, Scott
Mehzabeen, Nurjahan
Chowdhury, Wasimul Q.
Geanes, Eric S.
Battaile, Kevin P.
Roelofs, Jeroen
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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.
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Date
2014-04-01
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Publisher
Structural Biology Communications
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Keywords
Nas2, chaperones, Proteasome, PDZ domain
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