Top left: CryoEM map for the ATP-bound YbbAP at 3.6 Å resolution, and (below)ATP-bound YbbAP-TesA complex contoured to visualize the detergent belt. Maps are shown at two contour levels—a partially transparent low contour map is shown in white (4.5 σ), and a high contour map is shown colored by nearest protein chain (7 σ). Top right: Structures of apo YbbAP, ATP analogue-bound YbbAP, and ATP analogue-bound YbbAP-TesA. Proteins are shown in cartoon representation (YbbA green, YbbP teal, and TesA pink), and the non-hydrolyzable ATP analogue (AMP-PNP) is shown in blue atomic spheres. Bottom: Biological functions of the four Type VII ABC transporters in Escherichia coli. From left to right: YbbAP-TesA forms a novel type VII ABC transporter involved in extraction of hydrophobic compounds from the inner membrane and enzymatic hydrolysis in the periplasm; FtsEX-EnvC uses transmembrane conformational changes to regulate the activity of peptidoglycan amidases in the periplasm; MacAB-TolC drive efflux of antibiotics and small toxins across the outer membrane; and LolCDE extracts lipoproteins from the inner membrane and delivers them to the outer membrane via the LolA shuttle.
Structures of 3 of the 4 #Ecoli Type VII #ABCtransporter systems are known. @allistercrow.bsky.social &co use #cryoEM structures to show that the 4th, YbbAP, may extract hydrophobic compounds from the inner membrane & present them to periplasmic TesA for hydrolysis @plosbiology.org 🧪 plos.io/49EhNHD