8BMP
Cryo-EM structure of the folate-specific ECF transporter complex in MSP2N2 lipid nanodiscs bound to ATP and ADP
Summary for 8BMP
Entry DOI | 10.2210/pdb8bmp/pdb |
EMDB information | 16120 |
Descriptor | Energy-coupling factor transporter ATP-binding protein EcfA1, Energy-coupling factor transporter ATP-binding protein EcfA2, Folate family ECF transporter S component, ... (7 entities in total) |
Functional Keywords | abc transporter, ecf transporter complex, atp, adp, membrane protein |
Biological source | Lactobacillus delbrueckii subsp. bulgaricus ATCC 11842 = JCM 1002 More |
Total number of polymer chains | 4 |
Total formula weight | 116571.15 |
Authors | Thangaratnarajah, C.,Rheinberger, J.,Paulino, C.,Slotboom, D.J. (deposition date: 2022-11-10, release date: 2023-08-02, Last modification date: 2024-07-24) |
Primary citation | Thangaratnarajah, C.,Nijland, M.,Borges-Araujo, L.,Jeucken, A.,Rheinberger, J.,Marrink, S.J.,Souza, P.C.T.,Paulino, C.,Slotboom, D.J. Expulsion mechanism of the substrate-translocating subunit in ECF transporters. Nat Commun, 14:4484-4484, 2023 Cited by PubMed Abstract: Energy-coupling factor (ECF)-type transporters mediate the uptake of micronutrients in many bacteria. They consist of a substrate-translocating subunit (S-component) and an ATP-hydrolysing motor (ECF module) Previous data indicate that the S-component topples within the membrane to alternately expose the binding site to either side of the membrane. In many ECF transporters, the substrate-free S-component can be expelled from the ECF module. Here we study this enigmatic expulsion step by cryogenic electron microscopy and reveal that ATP induces a concave-to-convex shape change of two long helices in the motor, thereby destroying the S-component's docking site and allowing for its dissociation. We show that adaptation of the membrane morphology to the conformational state of the motor may favour expulsion of the substrate-free S-component when ATP is bound and docking of the substrate-loaded S-component after hydrolysis. Our work provides a picture of bilayer-assisted chemo-mechanical coupling in the transport cycle of ECF transporters. PubMed: 37491368DOI: 10.1038/s41467-023-40266-1 PDB entries with the same primary citation |
Experimental method | ELECTRON MICROSCOPY (3.2 Å) |
Structure validation
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