7Z2A
P. berghei kinesin-8B motor domain in no nucleotide state bound to tubulin dimer
Summary for 7Z2A
Entry DOI | 10.2210/pdb7z2a/pdb |
EMDB information | 14459 |
Descriptor | Detyrosinated tubulin alpha-1B chain, Tubulin beta chain, Kinesin-8, putative, ... (6 entities in total) |
Functional Keywords | kinesin, motor protein |
Biological source | Plasmodium berghei More |
Total number of polymer chains | 3 |
Total formula weight | 135838.63 |
Authors | Liu, T.,Shilliday, F.,Cook, A.D.,Moores, C.A. (deposition date: 2022-02-26, release date: 2022-10-19, Last modification date: 2024-07-17) |
Primary citation | Liu, T.,Shilliday, F.,Cook, A.D.,Zeeshan, M.,Brady, D.,Tewari, R.,Sutherland, C.J.,Roberts, A.J.,Moores, C.A. Mechanochemical tuning of a kinesin motor essential for malaria parasite transmission. Nat Commun, 13:6988-6988, 2022 Cited by PubMed Abstract: Plasmodium species cause malaria and kill hundreds of thousands annually. The microtubule-based motor kinesin-8B is required for development of the flagellated Plasmodium male gamete, and its absence completely blocks parasite transmission. To understand the molecular basis of kinesin-8B's essential role, we characterised the in vitro properties of kinesin-8B motor domains from P. berghei and P. falciparum. Both motors drive ATP-dependent microtubule gliding, but also catalyse ATP-dependent microtubule depolymerisation. We determined these motors' microtubule-bound structures using cryo-electron microscopy, which showed very similar modes of microtubule interaction in which Plasmodium-distinct sequences at the microtubule-kinesin interface influence motor function. Intriguingly however, P. berghei kinesin-8B exhibits a non-canonical structural response to ATP analogue binding such that neck linker docking is not induced. Nevertheless, the neck linker region is required for motility and depolymerisation activities of these motors. These data suggest that the mechanochemistry of Plasmodium kinesin-8Bs is functionally tuned to support flagella formation. PubMed: 36384964DOI: 10.1038/s41467-022-34710-x PDB entries with the same primary citation |
Experimental method | ELECTRON MICROSCOPY (4.3 Å) |
Structure validation
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