9E78

48-nm repeat of the Leishmania tarentolae doublet microtubule

This is a non-PDB format compatible entry.

Summary for 9E78

• Entry DOI: 10.2210/pdb9e78/pdb
• EMDB information: 47661
• Descriptor: Tubulin beta chain, CFAP53, CFAP67A, ... (74 entities in total)
• Functional Keywords: flagella, parasite, axoneme, doublet microtubule, structural protein
• Biological source: Leishmania tarentolae; More
• Total number of polymer chains: 491
• Total formula weight: 23444340.62

Authors

Doran, M.H.,Ren, P.,Hoog, J.L.,Brown, A. (deposition date: 2024-11-01, release date: 2025-03-12, Last modification date: 2025-03-26)

Primary citation

Doran, M.H.,Niu, Q.,Zeng, J.,Beneke, T.,Smith, J.,Ren, P.,Fochler, S.,Coscia, A.,Hoog, J.L.,Meleppattu, S.,Lishko, P.V.,Wheeler, R.J.,Gluenz, E.,Zhang, R.,Brown, A.
Evolutionary adaptations of doublet microtubules in trypanosomatid parasites.
Science, 387:eadr5507-eadr5507, 2025

PubMed Abstract: The movement and pathogenicity of trypanosomatid species, the causative agents of trypanosomiasis and leishmaniasis, are dependent on a flagellum that contains an axoneme of dynein-bound doublet microtubules (DMTs). In this work, we present cryo-electron microscopy structures of DMTs from two trypanosomatid species, and , at resolutions up to 2.7 angstrom. The structures revealed 27 trypanosomatid-specific microtubule inner proteins, a specialized dynein-docking complex, and the presence of paralogous proteins that enable higher-order periodicities or proximal-distal patterning. Leveraging the genetic tractability of trypanosomatid species, we quantified the location and contribution of each structure-identified protein to swimming behavior. Our study shows that proper B-tubule closure is critical for flagellar motility, exemplifying how integrating structural identification with systematic gene deletion can dissect individual protein contributions to flagellar motility.

PubMed: 40080577
DOI: 10.1126/science.adr5507

Experimental method

ELECTRON MICROSCOPY (2.9 Å)