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

The proteasome-assembly chaperone Nas2 binds to the proteasome subunit Rpt5 using its PDZ domain. The structure of the Nas2 PDZ domain has been determined. 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.
Authors:
 [1] ; ;  [2] ; ;  [1] ;  [3] ;  [1]
  1. Kansas State University, 338 Ackert Hall, Manhattan, KS 66506 (United States)
  2. University of Kansas, Del Shankel Structural Biology Center, Lawrence, KS 66047 (United States)
  3. IMCA-CAT Hauptman–Woodward Medical Research Institute, 9700 South Cass Avenue, Building 435A, Argonne, IL 60439 (United States)
Publication Date:
OSTI Identifier:
22375683
Resource Type:
Journal Article
Resource Relation:
Journal Name: Acta crystallographica. Section F, Structural biology communications; Journal Volume: 70; Journal Issue: Pt 4; Other Information: PMCID: PMC3976055; PMID: 24699731; PUBLISHER-ID: hv5251; OAI: oai:pubmedcentral.nih.gov:3976055; Copyright (c) Singh et al. 2014; This is an open-access article distributed under the terms of the Creative Commons Attribution Licence, which permits unrestricted use, distribution, and reproduction in any medium, provided the original authors and source are cited.; Country of input: International Atomic Energy Agency (IAEA)
Country of Publication:
United States
Language:
English
Subject:
97 MATHEMATICAL METHODS AND COMPUTING; 75 CONDENSED MATTER PHYSICS, SUPERCONDUCTIVITY AND SUPERFLUIDITY; BASES; FUNCTIONS; POLYPEPTIDES; RESOLUTION