7Z2C

P. falciparum kinesin-8B motor domain in no nucleotide bound to tubulin dimer

Summary for 7Z2C

• Entry DOI: 10.2210/pdb7z2c/pdb
• EMDB information: 14461
• Descriptor: Kinesin-like protein, Detyrosinated tubulin alpha-1B chain, Tubulin beta chain, ... (6 entities in total)
• Functional Keywords: kinesin, motor protein
• Biological source: Plasmodium falciparum (malaria parasite P. falciparum); More
• Total number of polymer chains: 3
• Total formula weight: 135889.70

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

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: 36384964
DOI: 10.1038/s41467-022-34710-x

Experimental method

ELECTRON MICROSCOPY (4.1 Å)