Crystal and Solution Structures of an HslUV Protease–Chaperone Complex

• Published in: Cell 2000-11, Vol.103 (4), p.633-643
• Main Authors: Sousa, Marcelo C., Trame, Christine B., Tsuruta, Hiro, Wilbanks, Sigurd M., Reddy, Vijay S., McKay, David B.
• Format: Article
• Language: English
• Subjects: Adenosine Triphosphatases - chemistry; ADVANCED LIGHT SOURCE; ADVANCED LIGHT SOURCE ALS; ATP-Dependent Proteases; Bacterial Proteins - chemistry; Cloning, Molecular; CRYSTAL STRUCTURE; Crystallography, X-Ray; Haemophilus influenzae - enzymology; Heat-Shock Proteins - chemistry; Hydrolysis; LAWRENCE BERKELEY LABORATORY; MATERIALS SCIENCE; Models, Molecular; Molecular Chaperones - chemistry; PARTICLE ACCELERATORS; Peptides - metabolism; Protein Structure, Quaternary; Recombinant Proteins - chemistry; Scattering, Radiation; Serine Endopeptidases - chemistry; Solutions
• ISSN: 0092-8674; 1097-4172
• DOI: 10.1016/S0092-8674(00)00166-5

HslUV is a “prokaryotic proteasome” composed of the HslV protease and the HslU ATPase, a chaperone of the Clp/Hsp100 family. The 3.4 Å crystal structure of an HslUV complex is presented here. Two hexameric ATP binding rings of HslU bind intimately to opposite sides of the HslV protease; the HslU “intermediate domains” extend outward from the complex. The solution structure of HslUV, derived from small angle X-ray scattering data under conditions where the complex is assembled and active, agrees with this crystallographic structure. When the complex forms, the carboxy-terminal helices of HslU distend and bind between subunits of HslV, and the apical helices of HslV shift substantially, transmitting a conformational change to the active site region of the protease.