Crystal and solution structures of an HsIUV protease-chaperone complex

Citation
Mc. Sousa et al., Crystal and solution structures of an HsIUV protease-chaperone complex, CELL, 103(4), 2000, pp. 633-643
Citations number
45
Categorie Soggetti
Cell & Developmental Biology
Journal title
CELL
ISSN journal
00928674 → ACNP
Volume
103
Issue
4
Year of publication
2000
Pages
633 - 643
Database
ISI
SICI code
0092-8674(20001110)103:4<633:CASSOA>2.0.ZU;2-5
Abstract
HslUV is a "prokaryotic proteasome" composed of the HslV protease and the H slU ATPase, a chaperone of the Clp/Hsp100 family. The 3.4 a crystal structu re of an HslUV complex is presented here. Two hexameric ATP binding rings o f HslU bind intimately to opposite sides of the HslV protease; the HslU "in termediate 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 crystallographi c structure. When the complex forms, the carboxy-terminal helices of HslU d istend and bind between subunits of HslV, and the apical helices of HsIV sh ift substantially, transmitting a conformational change to the active site region of the protease.