Abstract
Electron cryomicroscopy reveals an unprecedented conformation of the single-ring mutant of GroEL (SR398) bound to GroES in the presence of Mg-ATP. This conformation exhibits a considerable expansion of the folding cavity, with ∼80% more volume than the X-ray structure of the equivalent cis cavity in the GroEL-GroES-(ADP)7 complex. This expanded conformation can encapsulate an 86 kDa heterodimeric (αβ) assembly intermediate of mitochondrial branched-chain α-ketoacid dehydrogenase, the largest substrate ever observed to be cis encapsulated. The SR398-GroES-Mg-ATP complex is found to exist as a mixture of standard and expanded conformations, regardless of the absence or presence of the substrate. However, the presence of even a small substrate causes a pronounced bias toward the expanded conformation. Encapsulation of the large assembly intermediate is supported by a series of electron cryomicroscopy studies as well as the protection of both α and β subunits of the substrate from tryptic digestion.
Original language | English (US) |
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Pages (from-to) | 1711-1722 |
Number of pages | 12 |
Journal | Structure |
Volume | 14 |
Issue number | 11 |
DOIs | |
State | Published - Nov 2006 |
ASJC Scopus subject areas
- Structural Biology
- Molecular Biology