Structure, 2016, 24(4):537-546

Ring Separation Highlights the Protein-Folding Mechanism Used by the Phage EL-Encoded Chaperonin

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.

Molugu SK, Hildenbrand ZL, Morgan DG, Sherman MB, He L, Georgopoulos C, Sernova NV, Kurochkina LP, Mesyanzhinov VV, Miroshnikov KA, Bernal RA

IBCH: 3977
Ссылка на статью в журнале: https://linkinghub.elsevier.com/retrieve/pii/S0969212616000514
Кол-во цитирований на 03.2024: 12
Данные статьи проверены модераторами 2016-04-05