Luminescence resonance energy transfer spectroscopy of ATP-binding cassette proteins.

摘要: The ATP-binding cassette (ABC) superfamily includes regulatory and transport proteins. Most human ABC exporters pump substrates out of cells using energy from ATP hydrolysis. Although major advances have been made toward understanding the molecular mechanism exporters, there are still many issues unresolved. During last few years, luminescence resonance transfer has used to detect conformational changes in real time, with atomic resolution, isolated nucleotide binding domains (NBDs) full-length exporters. NBDs particularly interesting because they provide power stroke for substrate transport. Luminescence (LRET) is a spectroscopic technique that can dynamic information atomic-resolution protein under physiological conditions. Using LRET, it shown NBD dimerization, critical step proteins catalytic cycle, requires two sites. However, hydrolysis at just one sites drive dissociation dimer. It was also found bacterial exporter MsbA reconstituted lipid bilayer membrane studied 37°C never separate as much suggested by crystal structures. This observation stresses importance performing structural/functional studies physiologic article part Special Issue entitled: Beyond Structure-Function Horizon Membrane Proteins edited Ute Hellmich, Rupak Doshi Benjamin McIlwain.