Additional file 1 of Insights into the structure-function relationship of the NorQ/NorD chaperones from Paracoccus denitrificans reveal shared principles of interacting MoxR AAA+/VWA domain proteins

Additional file 1: Fig S1. SEC profiles. Fig S2. Comparison of VWA domains and the MIDAS region from different organisms. Fig S3. 2D class averages of NorQ in cryo-EM experiments. Fig S4. Sequence alignment, characteristics and homology model of NorQ. Fig S5. Prediction of disordered regions and overall architecture for full-length NorD from P. denitrificans. Fig S6. Finger-like protrusions predicted for several MoxR-associated VWA domains and pairwise alignments. Fig S7. AlphaFold-multimer model of the full-length NorD in complex with the NorQ hexamer. Fig S8. Superposition of the NorQ-VWA AlphaFold prediction and the fitted cryo-EM-model. Fig S9. Extra densities in the NorQWBD cryo-EM map. Fig S10. ATPase activity measurements. Fig S11. Sequence alignment of the NorB subunit of cNOR with NorZ (qNOR) from various organisms. Fig S12. Predicted VWA domain of NorD in comparison to several eukaryotic VWA domains. Fig S13. Structural connection between the “finger” and the MIDAS site in the NorD VWA domain. Table S1. Mass spectrometry analysis. Table S2. AlphaFold-multimer prediction datasets. Table S3. Re-activation experiments with cNOR using crude cell extracts. Table S4. Primers used in this study.