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Figure 2
The closed-like EhCRT structure reveals a complex conformational rearrangement. (a) Superposition of the open and closed EhCRT conformers focusing on the different junction and P conformations. The same colour code is used as in Fig. 1[link](a). The linker serine residue moves 26 Å away. (b, c) Side-by-side comparison of the open and closed states, with emphasis on the tilt of the P domain. The stable Trp and disulfide bond at the edge of the lectin-binding site (PBS) are shown on the right. (d) Details of the junction interaction in the closed conformation. (e, f) Comparative side-by-side views of the unusual conformational rearrangements in α1, J_N and β11.

IUCrJ
Volume 3| Part 6| November 2016| Pages 408-419
ISSN: 2052-2525
https://doi.org/10.1107/S2052252516012847