ABC transporters and the recruitment of a distal enzyme activity. Top left: a simplified schematic of the conventional ABC transporters, posited to switch between inward- and outward-facing states. ATP binding and hydrolysis drives the conformational switch and resetting the system. Bottom left: a schematic for the group that communicate conformational changes across the membrane, but do not form channels to displace transport substrates. Right: this schematic depicts the action of the system studied by McAndrew and colleagues, where the conformational propagation helps to deliver substrates to a captive and orientated enzyme—in this case, a hydrolytic esterase.
This Primer explores a @plosbiology.org study that reports #cryoEM structures of the #Ecoli Type VII #ABCtransporter system YbbAP-TesA, suggesting that YbbAP extracts hydrophobic compounds from the bacterial inner membrane 🧪 Paper: plos.io/49EhNHD Primer: plos.io/48ndzSq