Crystal and solution structures of an HslUV protease-chaperone complex.
HslUV is a "prokaryotic proteasome" composed of the HslV protease and the HslU ATPase, a chaperone of the Clp/Hsp100 family. The 3.4 A 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.
Sousa
M C
MC
Department of Structural Biology, Stanford University School of Medicine, Stanford, CA 94305, USA.
Trame
C B
CB
Tsuruta
H
H
Wilbanks
S M
SM
Reddy
V S
VS
McKay
D B
DB
D049069:ATP-Dependent Proteases; D000251:Adenosine Triphosphatases / Q000737:chemistry*; D001426:Bacterial Proteins / Q000737:chemistry*; D003001:Cloning, Molecular; D018360:Crystallography, X-Ray; D006193:Haemophilus influenzae / Q000201:enzymology; D006360:Heat-Shock Proteins / Q000737:chemistry*; D006868:Hydrolysis; D008958:Models, Molecular; D018832:Molecular Chaperones / Q000737:chemistry*; D010455:Peptides / Q000378:metabolism; D020836:Protein Structure, Quaternary; D011994:Recombinant Proteins / Q000737:chemistry; D012542:Scattering, Radiation; D012697:Serine Endopeptidases / Q000737:chemistry*; D012996:Solutions
D001426:Bacterial Proteins; D006360:Heat-Shock Proteins; D018832:Molecular Chaperones; D010455:Peptides; D011994:Recombinant Proteins; D012996:Solutions; D049069:ATP-Dependent Proteases; D012697:Serine Endopeptidases; D000251:Adenosine Triphosphatases