New publication: Gating Topology of the Proton-Coupled Oligopeptide Symporters

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This paper [?] is the result of a large collaboration between several groups. Since all the current crystal structures of peptide transporters are open to the cytoplasm (and hence closed to the periplasm), we wanted to investigate what bacterial peptide transporters (here PepTSo [?] and PepTSt [?]) looked like when they were open to the periplasm. We followed two tracks: first we built models of PepTSo and PepTSt in outward-open conformations using the repeat swapping method. The PepTSo model was validated using DEER spectroscopy. In the second track we ran unbiased molecular dynamics of both proteins with the hope that they might start to change conformation. To characterise the conformations of the transporter we systematically analysed all the known structures of major facilitator superfamily (MFS) transporter proteins which not only allowed us to classify the simulations but also show which helices in MFS transporters form the periplasmic and cytoplasmic gates.

The paper is free to download (open access) from the journal, Structure.

Update: the paper was chosen for the cover of the journal as you can see above,

References

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