Structural highlights
Function
PSMD9_YEAST Acts as a chaperone during the assembly of the 26S proteasome, specifically of the base subcomplex of the 19S regulatory complex (RC). During the base subcomplex assembly is part of a NAS2:RPT4:RPT5 module; NAS2 is released during the further base assembly process.
Publication Abstract from PubMed
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 A 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.
1.15 A resolution structure of the proteasome-assembly chaperone Nas2 PDZ domain.,Singh CR, Lovell S, Mehzabeen N, Chowdhury WQ, Geanes ES, Battaile KP, Roelofs J Acta Crystallogr F Struct Biol Commun. 2014 Apr;70(Pt 4):418-23. doi:, 10.1107/S2053230X14003884. Epub 2014 Mar 25. PMID:24699731[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Singh CR, Lovell S, Mehzabeen N, Chowdhury WQ, Geanes ES, Battaile KP, Roelofs J. 1.15 A resolution structure of the proteasome-assembly chaperone Nas2 PDZ domain. Acta Crystallogr F Struct Biol Commun. 2014 Apr;70(Pt 4):418-23. doi:, 10.1107/S2053230X14003884. Epub 2014 Mar 25. PMID:24699731 doi:http://dx.doi.org/10.1107/S2053230X14003884
