1NED

CRYSTAL STRUCTURE OF HSLV (CLPQ) AT 3.8 ANGSTROMS RESOLUTION

1NED の概要

• エントリーDOI: 10.2210/pdb1ned/pdb
• 分子名称: HSLV (1 entity in total)
• 機能のキーワード: hslv, clpq, hslvu, clpqy, atp-dependent protease, proteasome, hydrolase
• 由来する生物種: Escherichia coli
• 細胞内の位置: Cytoplasm: P0A7B8
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 60275.43

構造登録者

Bochtler, M.,Ditzel, L.,Groll, M.,Huber, R. (登録日: 1997-04-04, 公開日: 1998-04-08, 最終更新日: 2024-02-14)

主引用文献

Bochtler, M.,Ditzel, L.,Groll, M.,Huber, R.
Crystal structure of heat shock locus V (HslV) from Escherichia coli.
Proc.Natl.Acad.Sci.USA, 94:6070-6074, 1997

PubMed Abstract: Heat shock locus V (HslV; also called ClpQ) is the proteolytic core of the ATP-dependent protease HslVU in Escherichia coli. It has sequence similarity with the beta-type subunits of the eukaryotic and archaebacterial proteasomes. Unlike these particles, which display 72-point symmetry, it is a dimer of hexamers with 62-point symmetry. The crystal structure of HslV at 3.8-A resolution, determined by isomorphous replacement and symmetry averaging, shows that in spite of the different symmetry of the particle, the fold and the contacts between subunits are conserved. A tripeptide aldehyde inhibitor, acetyl-Leu-Leu-norleucinal, binds to the N-terminal threonine residue of HslV, probably as a hemiacetal, relating HslV also functionally to the proteasomes of archaea and eukaryotes.

PubMed: 9177170
DOI: 10.1073/pnas.94.12.6070

実験手法

X-RAY DIFFRACTION (3.8 Å)