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Literature summary for 5.6.1.7 extracted from

  • Clare, D.K.; Vasishtan, D.; Stagg, S.; Quispe, J.; Farr, G.W.; Topf, M.; Horwich, A.L.; Saibil, H.R.
    ATP-triggered conformational changes delineate substrate-binding and -folding mechanics of the GroEL chaperonin (2012), Cell, 149, 113-123.
    View publication on PubMedView publication on EuropePMC
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Protein Variants

Protein Variants Comment Organism
D398A to explore the multiple conformations induced upon ATP binding to GroEL a mutant is used. Mutant shows normal ATP binding but 3% of the wild-type steady-state ATPase activity. Statistical analysis of a large data set of single-particle cryo-EM images of mutant is carried out: multiple pre-hydrolysis conformations are resolved that can be ordered into a sequence to trace out smooth trajectories of domain movements for GroEL-ATP7 and GroEL-ATP14 complexes. The structures reveal a set of salt-bridge changes that provide a series of click stops (preferred conformations) on a trajectory to a conformation in which the apical domains are separated from each other and partially elevated but lack the full elevation and large clockwise twist seen in the GroES bound rings. This elevated, open conformation of the GroEL ring positions the GroES-binding sites on its apical surface, while still exposing key hydrophobic sites toward the cavity Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
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Synonyms

Synonyms Comment Organism
GroEL chaperonin
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 Escherichia coli