Article
A comparative electron paramagnetic resonance study of the nucleotide-binding domains' catalytic cycle in the assembled maltose ATP-binding cassette importer.
Biophysical journal - 15 Sept 2008
Grote Mathias, Bordignon Enrica, Polyhach Yevhen, Jeschke Gunnar, Steinhoff Heinz-Jürgen, Schneider Erwin
Abstract excerpt
We present a quantitative analysis of conformational changes of the nucleotide-binding subunits, MalK(2), of the maltose ATP-binding cassette importer MalFGK(2) during the transport cycle. Distance changes occurring between selected residues were monitored in the full transporter by site-directed spin-labeling electron paramagnetic resonance spectroscopy and site-directed chemical cross-linking. We considered...
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