1NED

CRYSTAL STRUCTURE OF HSLV (CLPQ) AT 3.8 ANGSTROMS RESOLUTION

Summary for 1NED

• Entry DOI: 10.2210/pdb1ned/pdb
• Descriptor: HSLV (1 entity in total)
• Functional Keywords: hslv, clpq, hslvu, clpqy, atp-dependent protease, proteasome, hydrolase
• Biological source: Escherichia coli
• Cellular location: Cytoplasm: P0A7B8
• Total number of polymer chains: 3
• Total formula weight: 60275.43

Authors

Bochtler, M.,Ditzel, L.,Groll, M.,Huber, R. (deposition date: 1997-04-04, release date: 1998-04-08, Last modification date: 2024-02-14)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (3.8 Å)