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. 2023 May 30;13:100. doi: 10.1186/s13578-023-01037-z

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© The Author(s) 2023

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this licence, visit http://creativecommons.org/licenses/by/4.0/. The Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated in a credit line to the data.

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Fig. 3 — Contact of hexamer in human PRPS2 filament. A and B Maps and models of human PRPS2 filament between adjacent hexamers. The residues responsible for the interactions are indicated. The area marked in red is that shown in Figure B. C Negative staining of human PRPS filament. The wild-type human PRPS2 can form filament under ADP + Mg²⁺, ATP + R5P + Pi + Mg²⁺,or Pi + PRPP + Mg²⁺ condition. Mutant R301A and R302A can disrupt filament formation. The scale bar is 200 nm. D Enzyme activity assay of wild-type human PRPS2 and its mutant. Mutant R301A and R302A almost lost its activity