Abstract
The structural biology of the exporter class of ABC transporters has witnessed rapid advances owing to a deluge of cryoEM structures ranging from single snapshots of substrate- or ATP-bound structures to the complement of structures populated under ATP turnover conditions. However, long standing mechanistic gaps remain including the sequence of events linking ATP hydrolysis in the nucleotide binding domains (NBDs) to isomerization of the transmembrane domains (TMD) and how substrate binding stimulates ATP hydrolysis.
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