4O06

1.15A Resolution Structure of the Proteasome Assembly Chaperone Nas2 PDZ Domain

4O06 の概要

• エントリーDOI: 10.2210/pdb4o06/pdb
• 分子名称: Probable 26S proteasome regulatory subunit p27, TETRAETHYLENE GLYCOL, SULFATE ION, ... (4 entities in total)
• 機能のキーワード: nas2, chaperone, proteasome, pdz domain
• 由来する生物種: Saccharomyces cerevisiae (Baker's yeast)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 11934.74

構造登録者

Lovell, S.,Mehzabeen, N.,Battaile, K.P.,Singh, C.R.,Chowdhury, W.Q.,Geanes, E.,Roelofs, J. (登録日: 2013-12-13, 公開日: 2014-04-16, 最終更新日: 2023-09-20)

主引用文献

Singh, C.R.,Lovell, S.,Mehzabeen, N.,Chowdhury, W.Q.,Geanes, E.S.,Battaile, K.P.,Roelofs, J.
1.15 angstrom resolution structure of the proteasome-assembly chaperone Nas2 PDZ domain.
Acta Crystallogr F Struct Biol Commun, 70:418-423, 2014

PubMed 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.

PubMed: 24699731
DOI: 10.1107/S2053230X14003884

実験手法

X-RAY DIFFRACTION (1.15 Å)