Estimating the true stability of the prehydrolytic outward-facing state in an ABC protein.

Abstract excerpt

CFTR, the anion channel mutated in cystic fibrosis patients, is a model ABC protein whose ATP-driven conformational cycle is observable at single-molecule level in patch-clamp recordings. Bursts of CFTR pore openings are coupled to tight dimerization of its two nucleotide-binding domains (NBDs) and in wild-type (WT) channels are mostly terminated by ATP hydrolysis. The slow rate of non-hydrolytic closure - which...

Topics

• Humans
• Cystic Fibrosis Transmembrane Conductance Regulator
• Adenosine Triphosphate
• Ion Channel Gating
• Mutation
• Catalytic Domain