9E5C
Cryo-EM structure of 96 nm repeat of microtubule doublet from T. brucei flagellum
This is a non-PDB format compatible entry.
Summary for 9E5C
| Entry DOI | 10.2210/pdb9e5c/pdb |
| EMDB information | 47524 |
| Descriptor | EF-hand domain-containing family member C2, LIM zinc-binding domain-containing protein, Dynein heavy chain, putative, ... (160 entities in total) |
| Functional Keywords | flagella, microtubule, motor protein |
| Biological source | Trypanosoma brucei brucei TREU927 More |
| Total number of polymer chains | 1166 |
| Total formula weight | 63727105.21 |
| Authors | Xia, X.,Shimogawa, M.M.,Wang, H.,Liu, S.,Wijono, A.,Langousis, G.,Kassem, A.M.,Wohlschlegel, J.A.,Hill, K.,Zhou, Z.H. (deposition date: 2024-10-28, release date: 2025-03-12, Last modification date: 2025-03-26) |
| Primary citation | Xia, X.,Shimogawa, M.M.,Wang, H.,Liu, S.,Wijono, A.,Langousis, G.,Kassem, A.M.,Wohlschlegel, J.A.,Hill, K.L.,Zhou, Z.H. Trypanosome doublet microtubule structures reveal flagellum assembly and motility mechanisms. Science, 387:eadr3314-eadr3314, 2025 Cited by PubMed Abstract: The flagellum of drives the parasite's characteristic screw-like motion and is essential for its replication, transmission, and pathogenesis. However, the molecular details of this process remain unclear. Here, we present high-resolution (up to 2.8 angstrom) cryo-electron microscopy structures of flagellar doublet microtubules (DMTs). Integrated modeling identified 154 different axonemal proteins inside and outside the DMT and, together with genetic and proteomic interrogation, revealed conserved and trypanosome-specific foundations of flagellum assembly and motility. We captured axonemal dynein motors in their pre-power stroke state. Comparing atomic models between pre- and post-power strokes defined how dynein structural changes drive sliding of adjacent DMTs during flagellar beating. This study illuminates structural dynamics underlying flagellar motility and identifies pathogen-specific proteins to consider for therapeutic interventions targeting neglected diseases. PubMed: 40080582DOI: 10.1126/science.adr3314 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.2 Å) |
Structure validation
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