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. 2019 Jun 28;10:2872. doi: 10.1038/s41467-019-10918-2

Fig. 4.

Fig. 4

Polypeptide substrate in SecA. a Top view of the SecA-SecY-substrate complex, showing polypeptide entry into SecA. The SecY channel is underneath SecA and not shown. Substrate density is shown in green. The conserved Arg367 in the PPXD loop is indicated as a red dot. b Close-up view of the β-sheet formed by substrate binding. The connecting β-strands at the back of the clamp are in shown in cyan, the PPXD β-strand in magenta, and the β-strand formed by the substrate in green. c SecA residues surrounding the polypeptide substrate are shown as sticks. Hydrophilic and hydrophobic residues, clustered on different sides, are highlighted with orange and purple dashed curves. d Interaction of the connecting β strands with different peptides. Shown is a superposition of different structures, in which β-strands were induced. The alignment is based on the connecting β-strands. The peptides are derived from (1) the translocating peptide in the present structure (green); (2) a C-terminal SecA segment (orange, PDB 1M74); (3) three amino acids of a synthetic peptide (red, PDB 3JV2); and (4) a segment of NBD2 of a neighboring SecA molecule in the crystal (purple, PDB 2IBM)