Fig. 1: Trapping a TRAP transporter. | Nature Communications

Fig. 1: Trapping a TRAP transporter.

From: Conformational coupling of the sialic acid TRAP transporter HiSiaQM with its substrate binding protein HiSiaP

Fig. 1

The transport cycle of TRAP transporters as described in14 is depicted schematically in the middle of the figure. To trap the transporter in specific states, the stator and elevator domains were cross-linked by disulfide engineering to yield states 2* and 4*. The cartoon representations of HiSiaPQM on the left and right of the figure are AlphaFold2 models of the tripartite complex14. The individual domains of the transporter are colored as in the schematic (HiSiaP: red, HiSiaQM stator: blue, HiSiaQM elevator: yellow). Residues that were mutated to cysteines to form disulfide bonds are indicated by magenta spheres and the disulfide bond is shown as a magenta bar connecting the two residues. In state 2*, the bound Neu5Ac is shown as spheres. IFS: inward-facing state; OFS: outward-facing state; Neu5Ac: N-Acetylneuraminic acid.

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