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

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. Th...

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Autores principales: Singh, Chingakham R., Lovell, Scott, Mehzabeen, Nurjahan, Chowdhury, Wasimul Q., Geanes, Eric S., Battaile, Kevin P., Roelofs, Jeroen
Formato: Online Artículo Texto
Lenguaje:English
Publicado: International Union of Crystallography 2014
Materias:
Structural Communications
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3976055/
https://www.ncbi.nlm.nih.gov/pubmed/24699731
http://dx.doi.org/10.1107/S2053230X14003884
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author Singh, Chingakham R.
Lovell, Scott
Mehzabeen, Nurjahan
Chowdhury, Wasimul Q.
Geanes, Eric S.
Battaile, Kevin P.
Roelofs, Jeroen
author_facet Singh, Chingakham R.
Lovell, Scott
Mehzabeen, Nurjahan
Chowdhury, Wasimul Q.
Geanes, Eric S.
Battaile, Kevin P.
Roelofs, Jeroen
author_sort Singh, Chingakham R.
collection PubMed
description 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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spelling pubmed-39760552014-04-24 1.15 Å resolution structure of the proteasome-assembly chaperone Nas2 PDZ domain Singh, Chingakham R. Lovell, Scott Mehzabeen, Nurjahan Chowdhury, Wasimul Q. Geanes, Eric S. Battaile, Kevin P. Roelofs, Jeroen Acta Crystallogr F Struct Biol Commun Structural Communications 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. International Union of Crystallography 2014-03-25 /pmc/articles/PMC3976055/ /pubmed/24699731 http://dx.doi.org/10.1107/S2053230X14003884 Text en © Singh et al. 2014 http://creativecommons.org/licenses/by/2.0/uk/ 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.
spellingShingle Structural Communications
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
title 1.15 Å resolution structure of the proteasome-assembly chaperone Nas2 PDZ domain
title_full 1.15 Å resolution structure of the proteasome-assembly chaperone Nas2 PDZ domain
title_fullStr 1.15 Å resolution structure of the proteasome-assembly chaperone Nas2 PDZ domain
title_full_unstemmed 1.15 Å resolution structure of the proteasome-assembly chaperone Nas2 PDZ domain
title_short 1.15 Å resolution structure of the proteasome-assembly chaperone Nas2 PDZ domain
title_sort 1.15 å resolution structure of the proteasome-assembly chaperone nas2 pdz domain
topic Structural Communications
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3976055/
https://www.ncbi.nlm.nih.gov/pubmed/24699731
http://dx.doi.org/10.1107/S2053230X14003884
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