Novel cryo-EM structure of an ADP-bound GroEL-GroES complex.
Sci Rep
; 11(1): 18241, 2021 09 14.
Article
em En
| MEDLINE
| ID: mdl-34521893
ABSTRACT
The GroEL-GroES chaperonin complex is a bacterial protein folding system, functioning in an ATP-dependent manner. Upon ATP binding and hydrolysis, it undergoes multiple stages linked to substrate protein binding, folding and release. Structural methods helped to reveal several conformational states and provide more information about the chaperonin functional cycle. Here, using cryo-EM we resolved two nucleotide-bound structures of the bullet-shaped GroEL-GroES1 complex at 3.4 Å resolution. The main difference between them is the relative orientation of their apical domains. Both structures contain nucleotides in cis and trans GroEL rings; in contrast to previously reported bullet-shaped complexes where nucleotides were only present in the cis ring. Our results suggest that the bound nucleotides correspond to ADP, and that such a state appears at low ATPADP ratios.
Texto completo:
1
Base de dados:
MEDLINE
Assunto principal:
Difosfato de Adenosina
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Chaperonina 60
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Chaperonina 10
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Proteínas de Escherichia coli
Idioma:
En
Ano de publicação:
2021
Tipo de documento:
Article