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Crystal and solution structures of an HslUV protease-chaperone complex.

M C Sousa1, C B Trame, H Tsuruta

  • 1Department of Structural Biology, Stanford University School of Medicine, Stanford, CA 94305, USA.

Cell
|December 7, 2000
PubMed
Summary

The HslUV complex, a prokaryotic proteasome, reveals its structure through X-ray crystallography. This reveals how the HslU ATPase chaperone interacts with the HslV protease, altering its active site.

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Molecular Biology

Background:

  • HslUV is a prokaryotic proteasome, a crucial cellular machine for protein degradation.
  • It comprises the HslV protease and the HslU ATPase, a member of the Clp/Hsp100 chaperone family.

Purpose of the Study:

  • To determine the high-resolution structure of the HslUV complex.
  • To elucidate the structural basis for the interaction between HslU and HslV and its functional implications.

Main Methods:

  • X-ray crystallography was used to obtain the 3.4 Å crystal structure of the HslUV complex.
  • Small-angle X-ray scattering (SAXS) was employed to determine the solution structure of the active HslUV complex.

Main Results:

  • The structure shows two hexameric ATP-binding rings of HslU intimately associated with the HslV protease.
  • HslU's intermediate domains extend outward, while its carboxy-terminal helices interact with HslV subunits.
  • SAXS data confirmed the crystallographic model in solution, indicating structural stability.

Conclusions:

  • The HslUV complex adopts a specific architecture where HslU binding induces conformational changes in HslV.
  • These structural rearrangements, particularly in the apical helices of HslV, are transmitted to the protease's active site.
  • This provides a structural basis for the chaperone-mediated activation and regulation of the prokaryotic proteasome.