4O06

1.15A Resolution Structure of the Proteasome Assembly Chaperone Nas2 PDZ Domain

Summary for 4O06

• Entry DOI: 10.2210/pdb4o06/pdb
• Descriptor: Probable 26S proteasome regulatory subunit p27, TETRAETHYLENE GLYCOL, SULFATE ION, ... (4 entities in total)
• Functional Keywords: nas2, chaperone, proteasome, pdz domain
• Biological source: Saccharomyces cerevisiae (Baker's yeast)
• Total number of polymer chains: 1
• Total formula weight: 11934.74

Authors

Lovell, S.,Mehzabeen, N.,Battaile, K.P.,Singh, C.R.,Chowdhury, W.Q.,Geanes, E.,Roelofs, J. (deposition date: 2013-12-13, release date: 2014-04-16, Last modification date: 2023-09-20)

Primary citation

Singh, C.R.,Lovell, S.,Mehzabeen, N.,Chowdhury, W.Q.,Geanes, E.S.,Battaile, K.P.,Roelofs, J.
1.15 angstrom resolution structure of the proteasome-assembly chaperone Nas2 PDZ domain.
Acta Crystallogr F Struct Biol Commun, 70:418-423, 2014

PubMed 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.

PubMed: 24699731
DOI: 10.1107/S2053230X14003884

Experimental method

X-RAY DIFFRACTION (1.15 Å)