Berkeley Lab researchers identify structure of control element that causes protein misfolding

A team of researchers with the Lawrence Berkeley National Laboratory (Berkeley Lab), using the exceptionally bright and powerful x-ray beams of the Advanced Light Source, have determined the crystal structure of a critical control element within chaperonin, the protein complex responsible for the correct folding of other proteins. The incorrect or ‘misfolding’ of proteins has been linked to many diseases, including Alzheimer’s, Parkinson’s and some forms of cancer. “We identified, for the first time, a region within group II chaperonins we call the nucleotide-sensing loop, which detects the presence of the ATP molecules that fuel the chaperonin folding motion,” says Paul Adams, a bioengineer with Berkeley Lab’s Physical Biosciences Division and leading authority on x-ray crystallography who led this work. “We knew that ATP hydrolysis is important for promoting protein folding, but we did not know how ATP activity was sensed and communicated.”