Structural basis for nutrient-activated channel opening in bacterial spore germination receptors
Cofsky, J. C.; Ramirez-Guadiana, F. H.; Sobecks-Doherty, B. L.; Artzi, L.; Amon, J. D.; Gao, Y.; Dror, R.; del Marmol, J.; Rudner, D. Z.; Kruse, A. C.
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GerA-family germinant receptors were recently identified as ion channels that initiate germination of dormant bacterial spores in response to nutrients. Here we report 2.0-[A] cryo-electron microscopy structures of apo, agonist-bound, and antagonist-bound GerA, revealing a symmetric pentamer of heterotrimers. Signaling relies on two allosteric switches that radiate from the LeuT-type ligand-binding subunit in opposite directions, one away from the channel subunit and one directly toward it. A lipoprotein subunit reroutes the first switch and allosterically activates the second, promoting their convergence on the channel. Together, these rearrangements comprise a multipronged, cooperative signal transduction pathway that connects nutrient binding to pore opening in this new class of ligand-gated ion channels.
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