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.
Keywords:
Nas2; PDZ domain; chaperones; proteasome.
Publication types
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Research Support, N.I.H., Extramural
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, Non-P.H.S.
MeSH terms
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Adenosine Triphosphatases / chemistry
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Adenosine Triphosphatases / metabolism*
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Amino Acid Sequence
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Crystallization
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Crystallography, X-Ray / methods*
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Models, Molecular
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Molecular Chaperones / chemistry*
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Molecular Sequence Data
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PDZ Domains
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Protein Conformation
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Saccharomyces cerevisiae / metabolism*
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Saccharomyces cerevisiae Proteins / chemistry*
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Saccharomyces cerevisiae Proteins / metabolism
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Sequence Homology, Amino Acid
Substances
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Molecular Chaperones
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NAS2 protein, S cerevisiae
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Saccharomyces cerevisiae Proteins
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Adenosine Triphosphatases
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RPT5 protein, S cerevisiae