Crystal structure of heat shock locus V (HslV) from Escherichia coli
| dc.creator | Bochtler, Matthias | |
| dc.creator | Ditzel, Lars | |
| dc.creator | Groll, Michael | |
| dc.creator | Huber, Robert | |
| dc.date | 1997-06-10 | |
| dc.date.accessioned | 2026-08-02T20:21:34Z | |
| dc.description | 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. | |
| dc.identifier | https://pmc.ncbi.nlm.nih.gov/articles/PMC21002/ | |
| dc.identifier | https://pubmed.ncbi.nlm.nih.gov/9177170/ | |
| dc.identifier | https://doi.org/10.1073/pnas.94.12.6070 | |
| dc.identifier.uri | https://repo.dare.co.zw/handle/123456789/85948 | |
| dc.language | en | |
| dc.publisher | National Academy of Sciences | |
| dc.rights | Copyright © 1997, The National Academy of Sciences of the USA | |
| dc.source | Proc Natl Acad Sci U S A | |
| dc.subject | Biological Sciences | |
| dc.title | Crystal structure of heat shock locus V (HslV) from Escherichia coli | |
| dc.type | Text |