Hexameric ring structure of the ATPase domain of the membrane-integrated metalloprotease FtsH from Thermus thermophilus HB8.
Structure
; 10(10): 1415-23, 2002 Oct.
Article
em En
| MEDLINE
| ID: mdl-12377127
ABSTRACT
FtsH is a cytoplasmic membrane-integrated, ATP-dependent metalloprotease, which processively degrades both cytoplasmic and membrane proteins in concert with unfolding. The FtsH protein is divided into the N-terminal transmembrane region and the larger C-terminal cytoplasmic region, which consists of an ATPase domain and a protease domain. We have determined the crystal structures of the Thermus thermophilus FtsH ATPase domain in the nucleotide-free and AMP-PNP- and ADP-bound states, in addition to the domain with the extra preceding segment. Combined with the mapping of the putative substrate binding region, these structures suggest that FtsH internally forms a hexameric ring structure, in which ATP binding could cause a conformational change to facilitate transport of substrates into the protease domain through the central pore.
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Base de dados:
MEDLINE
Assunto principal:
Proteínas de Bactérias
/
Thermus thermophilus
/
Adenosina Trifosfatases
/
Proteínas de Membrana
Idioma:
En
Ano de publicação:
2002
Tipo de documento:
Article