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

Chingakham R. Singh; Scott Lovell; Nurjahan Mehzabeen; Wasimul Q. Chowdhury; Eric S. Geanes; Kevin P. Battaile; Jeroen Roelofs

doi:10.1107/S2053230X14003884

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

Chingakham R. Singh
, Scott Lovell
, Nurjahan Mehzabeen
, Wasimul Q. Chowdhury
, Eric S. Geanes
, Kevin P. Battaile
, Jeroen Roelofs

Research output: Contribution to journal › Article › peer-review

6 Scopus citations

Abstract

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.

Original language	English (US)
Pages (from-to)	418-423
Number of pages	6
Journal	Acta Crystallographica Section F: Structural Biology and Crystallization Communications
Volume	70
Issue number	4
DOIs	https://doi.org/10.1107/S2053230X14003884
State	Published - Apr 2014

All Science Journal Classification (ASJC) codes

Biophysics
Structural Biology
Biochemistry
Genetics
Condensed Matter Physics

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Cite this

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title = "1.15 {\AA} resolution structure of the proteasome-assembly chaperone Nas2 PDZ domain",

abstract = "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 {\AA} 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.",

author = "Singh, \{Chingakham R.\} and Scott Lovell and Nurjahan Mehzabeen and Chowdhury, \{Wasimul Q.\} and Geanes, \{Eric S.\} and Battaile, \{Kevin P.\} and Jeroen Roelofs",

year = "2014",

month = apr,

doi = "10.1107/S2053230X14003884",

language = "English (US)",

volume = "70",

pages = "418--423",

journal = "Acta Crystallographica Section F: Structural Biology and Crystallization Communications",

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publisher = "International Union of Crystallography",

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T1 - 1.15 Å resolution structure of the proteasome-assembly chaperone Nas2 PDZ domain

AU - Singh, Chingakham R.

AU - Lovell, Scott

AU - Mehzabeen, Nurjahan

AU - Chowdhury, Wasimul Q.

AU - Geanes, Eric S.

AU - Battaile, Kevin P.

AU - Roelofs, Jeroen

PY - 2014/4

Y1 - 2014/4

N2 - 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.

AB - 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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AN - SCOPUS:84905448136

SN - 1744-3091

VL - 70

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EP - 423

JO - Acta Crystallographica Section F: Structural Biology and Crystallization Communications

JF - Acta Crystallographica Section F: Structural Biology and Crystallization Communications

IS - 4

ER -

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

Abstract

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