Acta Crystallographica Section F

Structural Biology Communications

Volume 70, Part 4 (April 2014)

structural communications

Acta Cryst. (2014). F70, 418-423    [ doi:10.1107/S2053230X14003884 ]

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

C. R. Singh, S. Lovell, N. Mehzabeen, W. Q. Chowdhury, E. S. Geanes, K. P. Battaile and J. Roelofs

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.

PDB reference: 4o06

Keywords: Nas2; chaperones; proteasome; PDZ domain.

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[ doi:10.1107/S2053230X14003884/hv5251sup1.pdf ]
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