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. 2022 Nov 3;5:1176. doi: 10.1038/s42003-022-04120-2

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© The Author(s) 2022

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 license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license 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 license, visit http://creativecommons.org/licenses/by/4.0/.

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Fig. 4 — a MBP-NLRP3 wild type and two different Sensor 1 mutants were analyzed by RP-HPLC. The protein samples (3 µM) were incubated at 25 °C in the presence of 100 µM ATP and 5 mM MgCl₂. The relative amount of ATP (%) is shown on the y-axis and the time (min) on the x-axis. The amount of ATP was determined in 10 min intervals, integrated and normalized to 100% nucleotide. Sequence alignments and sequence logos of the labeled motifs and residues are shown for human NLRP1-14. b Hydrolysis analysis of MBP-NLRP3 Sensor 2 mutants performed similarly as in a. c ATP hydrolysis analysis of the P412A mutant. d ATP hydrolysis analysis of the R262W CAPS/Glu-switch mutant.