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-Structure paper
タイトル | Mechanochemical tuning of a kinesin motor essential for malaria parasite transmission. |
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ジャーナル・号・ページ | Nat Commun, Vol. 13, Issue 1, Page 6988, Year 2022 |
掲載日 | 2022年11月16日 |
著者 | Tianyang Liu / Fiona Shilliday / Alexander D Cook / Mohammad Zeeshan / Declan Brady / Rita Tewari / Colin J Sutherland / Anthony J Roberts / Carolyn A Moores / |
PubMed 要旨 | 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 ...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. |
リンク | Nat Commun / PubMed:36384964 / PubMed Central |
手法 | EM (単粒子) |
解像度 | 3.3 - 4.3 Å |
構造データ | EMDB-14459, PDB-7z2a: EMDB-14460, PDB-7z2b: EMDB-14461, PDB-7z2c: |
化合物 | ChemComp-GTP: ChemComp-MG: ChemComp-G2P: ChemComp-ANP: |
由来 |
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キーワード | MOTOR PROTEIN / kinesin |