PMID:22028884
| Citation |
Mizobata, T, Uemura, T, Isaji, K, Hirayama, T, Hongo, K and Kawata, Y (2011) Probing the functional mechanism of Escherichia coli GroEL using circular permutation. PLoS ONE 6:e26462 |
|---|---|
| Abstract |
The Escherichia coli chaperonin GroEL subunit consists of three domains linked via two hinge regions, and each domain is responsible for a specific role in the functional mechanism. Here, we have used circular permutation to study the structural and functional characteristics of the GroEL subunit. |
| Links |
PubMed PMC3196576 Online version:10.1371/journal.pone.0026462 |
| Keywords |
Amino Acid Sequence; Chaperonin 10/metabolism; Chaperonin 60/chemistry; Chaperonin 60/genetics; Chaperonin 60/metabolism; Escherichia coli/enzymology; Microscopy, Electron; Models, Molecular; Mutation; Protein Engineering/methods; Protein Structure, Tertiary; Protein Subunits/chemistry; Protein Subunits/genetics; Protein Subunits/metabolism; Thiosulfate Sulfurtransferase/metabolism |
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