Fig. 1: Conservation of the structure of the FliPQR export gate in the closed state. | Nature Communications

Fig. 1: Conservation of the structure of the FliPQR export gate in the closed state.

From: The substrate specificity switch FlhB assembles onto the export gate to regulate type three secretion

Fig. 1

a Cryo-EM volumes calculated in Relion using data from S. typhimurium FliPQR (left, EMD-4173), S. flexneri SctRST (centre left, SctR5S4T1 class10 (EMD-4734)), P. savastanoi FliPQR (centre right) and V. mimicus FliPQR (right). FliQ2 and FliQ4 are coloured orange and FliQ1, FliQ3 and FliQ5 are coloured red. b Immunodetection of SctUFLAG on western blottings of SDS-PAGE-separated crude membrane samples of the indicated S. typhimurium SctS pBpa mutants (denoted with X). Each sample is shown with and without UV-irradiation to induce photocrosslinking of pBpa to neighbouring interaction partners. c As in b, but testing interactions to SctU with pBpa in SctTand SctR. d Mapping of the confirmed contact points between FliPQR/SctRST and FlhB/SctU, including those previously identified19 on the structure of FliPQR (S. typhimurium) and a model with a fifth FliQ subunit, which is based on the structure of P. savastanoi FliPQR.

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