PMID:9177170
| Citation |
Bochtler, M, Ditzel, L, Groll, M and Huber, R (1997) Crystal structure of heat shock locus V (HslV) from Escherichia coli. Proc. Natl. Acad. Sci. U.S.A. 94:6070-4 |
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| 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. |
| Links | |
| Keywords |
ATP-Dependent Proteases; Adenosine Triphosphatases/biosynthesis; Adenosine Triphosphatases/chemistry; Amino Acid Sequence; Base Sequence; Cloning, Molecular; Crystallography, X-Ray/methods; Cysteine Endopeptidases/chemistry; DNA Primers; Endopeptidases/biosynthesis; Endopeptidases/chemistry; Escherichia coli/enzymology; Heat-Shock Proteins/biosynthesis; Heat-Shock Proteins/chemistry; Macromolecular Substances; Models, Molecular; Molecular Sequence Data; Multienzyme Complexes/chemistry; Polymerase Chain Reaction; Proteasome Endopeptidase Complex; Protein Conformation; Protein Structure, Secondary; Recombinant Proteins/biosynthesis; Recombinant Proteins/chemistry; Sequence Alignment; Sequence Homology, Amino Acid; Serine Endopeptidases; Thermoplasma/metabolism |
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