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Crystal and solution structures of an HslUV protease-chaperone complex

Academic Article
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Overview

authors

  • Sousa, M. C.
  • Trame, C. B.
  • Tsuruta, H.
  • Wilbanks, S. M.
  • Reddy, Vijay
  • McKay, Dianne

publication date

  • November 2000

journal

  • Cell  Journal

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.

subject areas

  • ATP-Dependent Proteases
  • Adenosine Triphosphatases
  • Bacterial Proteins
  • Cloning, Molecular
  • Crystallography, X-Ray
  • Haemophilus influenzae
  • Heat-Shock Proteins
  • Hydrolysis
  • Models, Molecular
  • Molecular Chaperones
  • Peptides
  • Protein Structure, Quaternary
  • Recombinant Proteins
  • Scattering, Radiation
  • Serine Endopeptidases
  • Solutions
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Identity

International Standard Serial Number (ISSN)

  • 0092-8674

Digital Object Identifier (DOI)

  • 10.1016/s0092-8674(00)00166-5

PubMed ID

  • 11106733
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Additional Document Info

start page

  • 633

end page

  • 643

volume

  • 103

issue

  • 4

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