Ontology highlight
ABSTRACT:
SUBMITTER: Molugu SK
PROVIDER: S-EPMC4823152 | biostudies-literature | 2016 Apr
REPOSITORIES: biostudies-literature
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]