Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

7Z2A

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

Summary for 7Z2A
Entry DOI10.2210/pdb7z2a/pdb
EMDB information14459
DescriptorDetyrosinated tubulin alpha-1B chain, Tubulin beta chain, Kinesin-8, putative, ... (6 entities in total)
Functional Keywordskinesin, motor protein
Biological sourcePlasmodium berghei
More
Total number of polymer chains3
Total formula weight135838.63
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 citationLiu, 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: 36384964
DOI: 10.1038/s41467-022-34710-x
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (4.3 Å)
Structure validation

226707

건을2024-10-30부터공개중

PDB statisticsPDBj update infoContact PDBjnumon