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TitleChaperonin complex with a newly folded protein encapsulated in the folding chamber.
Journal, issue, pagesNature, Vol. 457, Issue 7225, Page 107-110, Year 2009
Publish dateJan 1, 2009
AuthorsD K Clare / P J Bakkes / H van Heerikhuizen / S M van der Vies / H R Saibil /
PubMed AbstractA subset of essential cellular proteins requires the assistance of chaperonins (in Escherichia coli, GroEL and GroES), double-ring complexes in which the two rings act alternately to bind, ...A subset of essential cellular proteins requires the assistance of chaperonins (in Escherichia coli, GroEL and GroES), double-ring complexes in which the two rings act alternately to bind, encapsulate and fold a wide range of nascent or stress-denatured proteins. This process starts by the trapping of a substrate protein on hydrophobic surfaces in the central cavity of a GroEL ring. Then, binding of ATP and co-chaperonin GroES to that ring ejects the non-native protein from its binding sites, through forced unfolding or other major conformational changes, and encloses it in a hydrophilic chamber for folding. ATP hydrolysis and subsequent ATP binding to the opposite ring trigger dissociation of the chamber and release of the substrate protein. The bacteriophage T4 requires its own version of GroES, gp31, which forms a taller folding chamber, to fold the major viral capsid protein gp23 (refs 16-20). Polypeptides are known to fold inside the chaperonin complex, but the conformation of an encapsulated protein has not previously been visualized. Here we present structures of gp23-chaperonin complexes, showing both the initial captured state and the final, close-to-native state with gp23 encapsulated in the folding chamber. Although the chamber is expanded, it is still barely large enough to contain the elongated gp23 monomer, explaining why the GroEL-GroES complex is not able to fold gp23 and showing how the chaperonin structure distorts to enclose a large, physiological substrate protein.
External linksNature / PubMed:19122642 / PubMed Central
MethodsEM (single particle)
Resolution10.1 - 10.7 Å
Structure data

EMDB-1544:
Structure of a chaperonin complex with non-native substrate protein gp23
Method: EM (single particle) / Resolution: 10.7 Å

EMDB-1545:
Structure of a chaperonin complex with non-native substrate protein gp23
Method: EM (single particle) / Resolution: 10.3 Å

EMDB-1546:
Structure of GroEL in complex with Bacteriophage T4 co-chaperone gp31 and ADPAlF3
Method: EM (single particle) / Resolution: 10.5 Å

EMDB-1547:
Structure of GroEL in complex with non-native capsid protein gp23, Bacteriophage T4 co-chaperone gp31 and ADPAlF3
Method: EM (single particle) / Resolution: 10.2 Å

EMDB-1548:
Structure of GroEL in complex with non-native capsid protein gp23, folding capsid protein gp23, Bacteriophage T4 co-chaperone gp31 and ADPAlF3
Method: EM (single particle) / Resolution: 10.1 Å

Source
  • Escherichia coli (E. coli)
  • Enterobacteria phage T4 (virus)
  • synthetic construct (others)

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