Crystal and solution structures of an HslUV protease-chaperone complex.
Cell
; 103(4): 633-43, 2000 Nov 10.
Article
em En
| MEDLINE
| ID: mdl-11106733
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.
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Proteínas de Bactérias
/
Serina Endopeptidases
/
Adenosina Trifosfatases
/
Chaperonas Moleculares
/
Proteínas de Choque Térmico
Idioma:
En
Revista:
Cell
Ano de publicação:
2000
Tipo de documento:
Article
País de afiliação:
Estados Unidos