6ZG3
the structure of ECF PanT transporter in a complex with a nanobody
Summary for 6ZG3
Entry DOI | 10.2210/pdb6zg3/pdb |
Related | 5JSZ 6FNP |
Descriptor | Energy-coupling factor transporter ATP-binding protein EcfA1, Energy-coupling factor transporter ATP-binding protein EcfA2, Conserved hypothetical membrane protein, ... (8 entities in total) |
Functional Keywords | ecf transporter, vitamin transport, pantothenate, membrane protein, transport protein |
Biological source | Lactobacillus delbrueckii subsp. bulgaricus ATCC 11842 = JCM 1002 More |
Total number of polymer chains | 10 |
Total formula weight | 271253.20 |
Authors | Setyawati, I.,Guskov, A.,Slotboom, D.J. (deposition date: 2020-06-18, release date: 2021-03-03, Last modification date: 2024-01-24) |
Primary citation | Setyawati, I.,Stanek, W.K.,Majsnerowska, M.,Swier, L.J.Y.M.,Pardon, E.,Steyaert, J.,Guskov, A.,Slotboom, D.J. In vitro reconstitution of dynamically interacting integral membrane subunits of energy-coupling factor transporters. Elife, 9:-, 2020 Cited by PubMed Abstract: Energy-coupling factor (ECF) transporters mediate import of micronutrients in prokaryotes. They consist of an integral membrane S-component (that binds substrate) and ECF module (that powers transport by ATP hydrolysis). It has been proposed that different S-components compete for docking onto the same ECF module, but a minimal liposome-reconstituted system, required to substantiate this idea, is lacking. Here, we co-reconstituted ECF transporters for folate (ECF-FolT2) and pantothenate (ECF-PanT) into proteoliposomes, and assayed for crosstalk during active transport. The kinetics of transport showed that exchange of S-components is part of the transport mechanism. Competition experiments suggest much slower substrate association with FolT2 than with PanT. Comparison of a crystal structure of ECF-PanT with previously determined structures of ECF-FolT2 revealed larger conformational changes upon binding of folate than pantothenate, which could explain the kinetic differences. Our work shows that a minimal in vitro system with two reconstituted transporters recapitulates intricate kinetics behaviour observed in vivo. PubMed: 33350937DOI: 10.7554/eLife.64389 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.8 Å) |
Structure validation
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