title: Crystal structure of heat shock locus V (HslV) from Escherichia coli.
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.
authors.affiliation: Max-Planck-Institut für Biochemie, Am Klopferspitz 18a, D-82152 Martinsried, Germany.
authors.forename: M
authors.initials: M
authors.lastname: Bochtler
authors.forename: L
authors.initials: L
authors.lastname: Ditzel
authors.forename: M
authors.initials: M
authors.lastname: Groll
authors.forename: R
authors.initials: R
authors.lastname: Huber
mesh_terms: D049069:ATP-Dependent Proteases; D000251:Adenosine Triphosphatases / Q000096:biosynthesis / Q000737:chemistry*; D000595:Amino Acid Sequence; D001483:Base Sequence; D003001:Cloning, Molecular; D018360:Crystallography, X-Ray / Q000379:methods; D003546:Cysteine Endopeptidases / Q000737:chemistry*; D017931:DNA Primers; D010450:Endopeptidases / Q000096:biosynthesis / Q000737:chemistry*; D004926:Escherichia coli / Q000201:enzymology*; D006360:Heat-Shock Proteins / Q000096:biosynthesis / Q000737:chemistry; D046911:Macromolecular Substances; D008958:Models, Molecular; D008969:Molecular Sequence Data; D009097:Multienzyme Complexes / Q000737:chemistry*; D016133:Polymerase Chain Reaction; D046988:Proteasome Endopeptidase Complex; D011487:Protein Conformation; D017433:Protein Structure, Secondary; D011994:Recombinant Proteins / Q000096:biosynthesis / Q000737:chemistry; D016415:Sequence Alignment; D017386:Sequence Homology, Amino Acid; D012697:Serine Endopeptidases; D013822:Thermoplasma / Q000378:metabolism
chemical_list: D017931:DNA Primers; D006360:Heat-Shock Proteins; D046911:Macromolecular Substances; D009097:Multienzyme Complexes; D011994:Recombinant Proteins; D010450:Endopeptidases; D049069:ATP-Dependent Proteases; D012697:Serine Endopeptidases; D003546:Cysteine Endopeptidases; D046988:Proteasome Endopeptidase Complex; D000251:Adenosine Triphosphatases