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![[Figure 2]](ud5019fig2_combined_mag.jpg)
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Figure 2
Movements of conserved sequence motif III control the formation of a channel connecting the nucleotide-binding site to the protein surface. (a) In the ctPrp2–ADP-CF1 structure, motif III adopts a conformation that allows the formation of a channel that connects the γ-phosphate position of the active site to the exterior of the protein. In other ADP- and ADP-BeF3−-bound structures motif III closes this channel. The exit channel is highlighted as purple spheres. CF stands for crystal form. (b) Overview of motif III interactions in the ADP-bound state. (c) Overview of motif III interactions in the ADP-BeF3−-bound state. (d) Exemplary trajectory of the γ-phosphate through the exit channel based on MD calculations. (e) Only minor movements of motifs I and III allow trespassing of the γ-phosphate through the exit channel (green, ATP-bound state; red, moved motifs after MD calculations). |
![[Figure 2]](ud5019fig2_combined.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
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