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Structure paper

TitleCryo-EM structure of a microtubule-bound parasite kinesin motor and implications for its mechanism and inhibition.
Journal, issue, pagesJ Biol Chem, Vol. 297, Issue 5, Page 101063, Year 2021
Publish dateAug 8, 2021
AuthorsAlexander D Cook / Anthony J Roberts / Joseph Atherton / Rita Tewari / Maya Topf / Carolyn A Moores /
PubMed AbstractPlasmodium parasites cause malaria and are responsible annually for hundreds of thousands of deaths. Kinesins are a superfamily of microtubule-dependent ATPases that play important roles in the ...Plasmodium parasites cause malaria and are responsible annually for hundreds of thousands of deaths. Kinesins are a superfamily of microtubule-dependent ATPases that play important roles in the parasite replicative machinery, which is a potential target for antiparasite drugs. Kinesin-5, a molecular motor that cross-links microtubules, is an established antimitotic target in other disease contexts, but its mechanism in Plasmodium falciparum is unclear. Here, we characterized P. falciparum kinesin-5 (PfK5) using cryo-EM to determine the motor's nucleotide-dependent microtubule-bound structure and introduced 3D classification of individual motors into our microtubule image processing pipeline to maximize our structural insights. Despite sequence divergence in PfK5, the motor exhibits classical kinesin mechanochemistry, including ATP-induced subdomain rearrangement and cover neck bundle formation, consistent with its plus-ended directed motility. We also observed that an insertion in loop5 of the PfK5 motor domain creates a different environment in the well-characterized human kinesin-5 drug-binding site. Our data reveal the possibility for selective inhibition of PfK5 and can be used to inform future exploration of Plasmodium kinesins as antiparasite targets.
External linksJ Biol Chem / PubMed:34375637 / PubMed Central
MethodsEM (helical sym.)
Resolution4.0 - 4.4 Å
Structure data

12257

7nb8

EMDB-12257, PDB-7nb8:
Plasmodium falciparum kinesin-5 motor domain without nucleotide, complexed with 14 protofilament microtubule.
Method: EM (helical sym.) / Resolution: 4.4 Å

12258

7nba

EMDB-12258, PDB-7nba:
Plasmodium falciparum kinesin-5 motor domain bound to AMPPNP, complexed with 14 protofilament microtubule.
Method: EM (helical sym.) / Resolution: 4.0 Å

Chemicals

ChemComp-GTP:
GUANOSINE-5'-TRIPHOSPHATE / GTP, energy-carrying molecule*YM / Guanosine triphosphate

ChemComp-MG:
Unknown entry

ChemComp-G2P:
PHOSPHOMETHYLPHOSPHONIC ACID GUANYLATE ESTER / GMP-CPP, energy-carrying molecule analogue*YM

ChemComp-ANP:
PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER / AMP-PNP, energy-carrying molecule analogue*YM

Source
  • sus scrofa (pig)
  • plasmodium falciparum (isolate 3d7) (eukaryote)
  • Pig (pig)
  • plasmodium falciparum (isolate nf54) (eukaryote)
KeywordsMOTOR PROTEIN / Cytoskeleton / mitosis / mitotic

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