4o06 | pdb_00004o06

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

spinqualitylabelsall models 4o06, resolution 1.15Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4o06 is a 1 chain structure with sequence from Saccharomyces cerevisiae S288C. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.15Å Ligands: PG4, SO4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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