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TitleRing Separation Highlights the Protein-Folding Mechanism Used by the Phage EL-Encoded Chaperonin.
Journal, issue, pagesStructure, Vol. 24, Issue 4, Page 537-546, Year 2016
Publish dateApr 5, 2016
AuthorsSudheer K Molugu / Zacariah L Hildenbrand / David Gene Morgan / Michael B Sherman / Lilin He / Costa Georgopoulos / Natalia V Sernova / Lidia P Kurochkina / Vadim V Mesyanzhinov / Konstantin A Miroshnikov / Ricardo A Bernal /
PubMed AbstractChaperonins are ubiquitous, ATP-dependent protein-folding molecular machines that are essential for all forms of life. Bacteriophage φEL encodes its own chaperonin to presumably fold exceedingly ...Chaperonins are ubiquitous, ATP-dependent protein-folding molecular machines that are essential for all forms of life. Bacteriophage φEL encodes its own chaperonin to presumably fold exceedingly large viral proteins via profoundly different nucleotide-binding conformations. Our structural investigations indicate that ATP likely binds to both rings simultaneously and that a misfolded substrate acts as the trigger for ATP hydrolysis. More importantly, the φEL complex dissociates into two single rings resulting from an evolutionarily altered residue in the highly conserved ATP-binding pocket. Conformational changes also more than double the volume of the single-ring internal chamber such that larger viral proteins are accommodated. This is illustrated by the fact that φEL is capable of folding β-galactosidase, a 116-kDa protein. Collectively, the architecture and protein-folding mechanism of the φEL chaperonin are significantly different from those observed in group I and II chaperonins.
External linksStructure / PubMed:26996960 / PubMed Central
MethodsEM (single particle)
Resolution6.8 - 11.7 Å
Structure data

EMDB-6492:
Electron cryo-microscopy of bacteriophage EL chaperonin in the ATP-bound conformation
Method: EM (single particle) / Resolution: 6.8 Å

EMDB-6493:
Electron cryo-microscopy of bacteriophage EL chaperonin in the ADP-bound conformation
Method: EM (single particle) / Resolution: 11.7 Å

EMDB-6494:
Electron cryo-microscopy of bacteriophage EL chaperonin in the nucleotide-free conformation
Method: EM (single particle) / Resolution: 9.0 Å

Source
  • Pseudomonas phage EL (virus)

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