Crystal structure of heat shock locus V (HslV) from Escherichia coli
AUTOR(ES)
Bochtler, Matthias
FONTE
The National Academy of Sciences of the USA
RESUMO
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 β-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-Å 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.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=21002Documentos Relacionados
- Mutational studies on HslU and its docking mode with HslV
- Functional interactions of HslV (ClpQ) with the ATPase HslU (ClpY)
- Covalent modification of the active site threonine of proteasomal β subunits and the Escherichia coli homolog HslV by a new class of inhibitors
- Crystal structure of CspA, the major cold shock protein of Escherichia coli.
- Structure-function analysis of the Escherichia coli GrpE heat shock protein.
