Unknown

Dataset Information

0

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


ABSTRACT: Chaperonins are ubiquitous, ATP-dependent protein-folding molecular machines that are essential for all forms of life. Bacteriophage ?EL 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 ?EL 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 ?EL is capable of folding ?-galactosidase, a 116-kDa protein. Collectively, the architecture and protein-folding mechanism of the ?EL chaperonin are significantly different from those observed in group I and II chaperonins.

SUBMITTER: Molugu SK 

PROVIDER: S-EPMC4823152 | biostudies-literature | 2016 Apr

REPOSITORIES: biostudies-literature

altmetric image

Publications

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

Molugu Sudheer K SK   Hildenbrand Zacariah L ZL   Morgan David Gene DG   Sherman Michael B MB   He Lilin L   Georgopoulos Costa C   Sernova Natalia V NV   Kurochkina Lidia P LP   Mesyanzhinov Vadim V VV   Miroshnikov Konstantin A KA   Bernal Ricardo A RA  

Structure (London, England : 1993) 20160317 4


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 ri  ...[more]

Similar Datasets

| S-EPMC2834796 | biostudies-literature
| S-EPMC3829408 | biostudies-literature
| S-EPMC3132998 | biostudies-literature
| S-EPMC4071350 | biostudies-literature
| S-EPMC3456655 | biostudies-other
| S-EPMC7912344 | biostudies-literature
| S-EPMC5780408 | biostudies-literature
| S-EPMC5143341 | biostudies-literature
| S-EPMC6190516 | biostudies-literature
| S-EPMC2396394 | biostudies-literature