7QDW
Solution structure of the complex between plasmodial ZNHIT3 and NUFIP1 proteins
Summary for 7QDW
| Entry DOI | 10.2210/pdb7qdw/pdb |
| NMR Information | BMRB: 34693 |
| Descriptor | Zinc finger protein, putative, NUFIP1 domain-containing protein (2 entities in total) |
| Functional Keywords | pac-hit fold, jaw helices, signaling protein |
| Biological source | Plasmodium falciparum (isolate 3D7) More |
| Total number of polymer chains | 2 |
| Total formula weight | 11686.37 |
| Authors | Chagot, M.E.,Quinternet, M. (deposition date: 2021-11-30, release date: 2022-03-30, Last modification date: 2024-06-19) |
| Primary citation | Chagot, M.E.,Boutilliat, A.,Kriznik, A.,Quinternet, M. Structural Analysis of the Plasmodial Proteins ZNHIT3 and NUFIP1 Provides Insights into the Selectivity of a Conserved Interaction. Biochemistry, 61:479-493, 2022 Cited by PubMed Abstract: Malaria is a widespread and lethal disease caused by the parasites that can infect human beings through Anopheles mosquitoes. For that reason, the biology of needs to be studied to develop antimalarial treatments. By determining the three-dimensional structures of macromolecules, structural biology helps to understand the function of proteins and can reveal how interactions occur between biological partners. Here, we studied the ZNHIT3 and NUFIP1 proteins from , two proteins tightly linked to the ribosome biology. Due to their important functions in post-translational modifications of ribosomal RNAs and in ribophagy, these proteins participate in the survival of cells. In this study, we solved the three-dimensional structure of a thermally stable and species-dependent complex between fragments of these proteins. Our results were compared to the AlphaFold predictions, which motivated the study of the free ZNHIT3 fragment that binds NUFIP1. We showed that the latter fragment multimerized in vitro but also had the inner ability to change its conformation to escape the solvent exposition of key hydrophobic residues involved in the interaction with NUFIP1. Our data could open the gate to selective drug discovery processes involving these two proteins. PubMed: 35315277DOI: 10.1021/acs.biochem.1c00792 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
Download full validation report
