Crystal and solution structures of an HslUV protease-chaperone complex. Journal Article uri icon

Overview

abstract

  • 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.

publication date

  • November 1, 2000

Full Author List

  • Sousa MC; Trame CB; Tsuruta H; Wilbanks SM; Reddy VS; McKay DB

published in

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Additional Document Info

start page

  • 633

end page

  • 643

volume

  • 103

issue

  • 4