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

Abstract

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
Journal Name:
Acta crystallographica. Section F, Structural biology communications
Additional Journal Information:
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); Journal ID: ISSN 2053-230X
Country of Publication:
United States
Language:
English
Subject:
97 MATHEMATICAL METHODS AND COMPUTING; 75 CONDENSED MATTER PHYSICS, SUPERCONDUCTIVITY AND SUPERFLUIDITY; BASES; FUNCTIONS; POLYPEPTIDES; RESOLUTION

Citation Formats

Singh, Chingakham R., Lovell, Scott, Mehzabeen, Nurjahan, Chowdhury, Wasimul Q., Geanes, Eric S., Battaile, Kevin P., and Roelofs, Jeroen. 1.15 Å resolution structure of the proteasome-assembly chaperone Nas2 PDZ domain. United States: N. p., 2014. Web. doi:10.1107/S2053230X14003884.
Singh, Chingakham R., Lovell, Scott, Mehzabeen, Nurjahan, Chowdhury, Wasimul Q., Geanes, Eric S., Battaile, Kevin P., & Roelofs, Jeroen. 1.15 Å resolution structure of the proteasome-assembly chaperone Nas2 PDZ domain. United States. doi:10.1107/S2053230X14003884.
Singh, Chingakham R., Lovell, Scott, Mehzabeen, Nurjahan, Chowdhury, Wasimul Q., Geanes, Eric S., Battaile, Kevin P., and Roelofs, Jeroen. Tue . "1.15 Å resolution structure of the proteasome-assembly chaperone Nas2 PDZ domain". United States. doi:10.1107/S2053230X14003884.
@article{osti_22375683,
title = {1.15 Å resolution structure of the proteasome-assembly chaperone Nas2 PDZ domain},
author = {Singh, Chingakham R. and Lovell, Scott and Mehzabeen, Nurjahan and Chowdhury, Wasimul Q. and Geanes, Eric S. and Battaile, Kevin P. and Roelofs, Jeroen},
abstractNote = {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.},
doi = {10.1107/S2053230X14003884},
journal = {Acta crystallographica. Section F, Structural biology communications},
issn = {2053-230X},
number = Pt 4,
volume = 70,
place = {United States},
year = {2014},
month = {3}
}