TY - JOUR
T1 - 1.15 Å resolution structure of the proteasome-assembly chaperone Nas2 PDZ domain
AU - Singh, Chingakham R.
AU - Lovell, Scott
AU - Mehzabeen, Nurjahan
AU - Chowdhury, Wasimul Q.
AU - Geanes, Eric S.
AU - Battaile, Kevin P.
AU - Roelofs, Jeroen
PY - 2014/4
Y1 - 2014/4
N2 - 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.
AB - 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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U2 - 10.1107/S2053230X14003884
DO - 10.1107/S2053230X14003884
M3 - Article
C2 - 24699731
AN - SCOPUS:84905448136
SN - 1744-3091
VL - 70
SP - 418
EP - 423
JO - Acta Crystallographica Section F:Structural Biology Communications
JF - Acta Crystallographica Section F:Structural Biology Communications
IS - 4
ER -