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.
journal_name
Proc Natl Acad Sci U S Aauthors
Bochtler M,Ditzel L,Groll M,Huber Rdoi
10.1073/pnas.94.12.6070subject
Has Abstractpub_date
1997-06-10 00:00:00pages
6070-4issue
12eissn
0027-8424issn
1091-6490journal_volume
94pub_type
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