Covalently linked HslU hexamers support a probabilistic mechanism that links ATP hydrolysis to protein unfolding and translocation.

Baytshtok, Vladimir; Chen, Jiejin; Glynn, Steven E; Nager, Andrew R; Grant, Robert A; Baker, Tania A; Sauer, Robert T

Baytshtok, Vladimir; Chen, Jiejin; Glynn, Steven E; Nager, Andrew R; Grant, Robert A; Baker, Tania A; Sauer, Robert T.

Afiliação

Baytshtok V; From the Department of Biology and.
Chen J; From the Department of Biology and.
Glynn SE; From the Department of Biology and.
Nager AR; From the Department of Biology and.
Grant RA; From the Department of Biology and.
Baker TA; From the Department of Biology and.
Sauer RT; Howard Hughes Medical Institute, Massachusetts Institute of Technology, Cambridge, Massachusetts 02139.

J Biol Chem ; 292(14): 5695-5704, 2017 04 07.

Article em En | MEDLINE | ID: mdl-28223361

Assuntos

Trifosfato de Adenosina/química; Endopeptidase Clp/química; Proteínas de Escherichia coli/química; Escherichia coli/enzimologia; Desdobramento de Proteína; Trifosfato de Adenosina/genética; Trifosfato de Adenosina/metabolismo; Domínio Catalítico; Endopeptidase Clp/genética; Endopeptidase Clp/metabolismo; Escherichia coli/genética; Proteínas de Escherichia coli/genética; Proteínas de Escherichia coli/metabolismo

Palavras-chave

AAA+ protease; ATP-dependent protease; ATPases associated with diverse cellular activities (AAA); HslUV; crystal structure; mixed hexameric rings; protein degradation; protein engineering; protein turnover; protein unfolding

Texto completo

Imprimir

XML

PubMed Links

Buscar no Google

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Trifosfato de Adenosina / Proteínas de Escherichia coli / Endopeptidase Clp / Escherichia coli / Desdobramento de Proteína Idioma: En Revista: J Biol Chem Ano de publicação: 2017 Tipo de documento: Article

Texto completo

Imprimir

XML

PubMed Links

Buscar no Google