期刊
ELIFE
卷 8, 期 -, 页码 -出版社
ELIFE SCIENCES PUBLICATIONS LTD
DOI: 10.7554/eLife.44652
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资金
- European Commission [638536]
- Deutsche Forschungsgemeinschaft [GRK2062/1, SFB863]
- National Health and Medical Research Council [1080784, 1122582]
- Nederlandse Organisatie voor Wetenschappelijk Onderzoek [722.012.012]
- H2020 European Research Council ERC [670578]
- Australian Research Council [DP170102102, FT170100006]
- European Molecular Biology Organization [ALF 47-2012]
- European Research Council (ERC) [638536] Funding Source: European Research Council (ERC)
- Australian Research Council [FT170100006] Funding Source: Australian Research Council
- National Health and Medical Research Council of Australia [1122582, 1080784] Funding Source: NHMRC
Substrate-binding proteins (SBPs) are associated with ATP-binding cassette importers and switch from an open to a closed conformation upon substrate binding, providing specificity for transport. We investigated the effect of substrates on the conformational dynamics of six SBPs and the impact on transport. Using single-molecule FRET, we reveal an unrecognized diversity of plasticity in SBPs. We show that a unique closed SBP conformation does not exist for transported substrates. Instead, SBPs sample a range of conformations that activate transport. Certain nontransported ligands leave the structure largely unaltered or trigger a conformation distinct from that of transported substrates. Intriguingly, in some cases, similar SBP conformations are formed by both transported and non-transported ligands. In this case, the inability for transport arises from slow opening of the SBP or the selectivity provided by the translocator. Our results reveal the complex interplay between ligand-SBP interactions, SBP conformational dynamics and substrate transport.
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