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. Author manuscript; available in PMC: 2023 Sep 1.
Published in final edited form as: Nat Struct Mol Biol. 2023 Feb 6;30(3):391–402. doi: 10.1038/s41594-023-00921-z

Figure 5. Filament formation stabilizes the C-terminus and allosteric site.

Figure 5.

A. The allosteric site and C-terminus of PRPS1 in the presence of phosphate, ATP, and ribose-5-phosphate. B. The allosteric site and C-terminus of PRPS1-E307A. C. The allosteric site and C-terminus of PRPS1 in the presence of phosphate and ADP. D. The allosteric site and C-terminus of PRPS1-E307A in the presence of phosphate and ADP. E. The PRPS1-E307A dataset was symmetry expanded and classified without alignment on a masked protomer, and two volumes were locally refined. Top. Map and model of the PRPS1-E307A showing the presence of the C-terminus and ADP bound in the allosteric site. Bottom. Map and model of the PRPS1-E307A lacking ADP in the allosteric site and a bound C-terminus.