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TitleCryo-EM structure of the Ustilago maydis kinesin-5 motor domain bound to microtubules.
Journal, issue, pagesJ Struct Biol, Vol. 207, Issue 3, Page 312-316, Year 2019
Publish dateSep 1, 2019
AuthorsOttilie von Loeffelholz / Carolyn Ann Moores /
PubMed AbstractIn many eukaryotes, kinesin-5 motors are essential for mitosis, and small molecules that inhibit human kinesin-5 disrupt cell division. To investigate whether fungal kinesin-5s could be targets for ...In many eukaryotes, kinesin-5 motors are essential for mitosis, and small molecules that inhibit human kinesin-5 disrupt cell division. To investigate whether fungal kinesin-5s could be targets for novel fungicides, we studied kinesin-5 from the pathogenic fungus Ustilago maydis. We used cryo-electron microscopy to determine the microtubule-bound structure of its motor domain with and without the N-terminal extension. The ATP-like conformations of the motor in the presence or absence of this N-terminus are very similar, suggesting this region is structurally disordered and does not directly influence the motor ATPase. The Ustilago maydis kinesin-5 motor domain adopts a canonical ATP-like conformation, thereby allowing the neck linker to bind along the motor domain towards the microtubule plus end. However, several insertions within this motor domain are structurally distinct. Loop2 forms a non-canonical interaction with α-tubulin, while loop8 may bridge between two adjacent protofilaments. Furthermore, loop5 - which in human kinesin-5 is involved in binding allosteric inhibitors - protrudes above the nucleotide binding site, revealing a distinct binding pocket for potential inhibitors. This work highlights fungal-specific elaborations of the kinesin-5 motor domain and provides the structural basis for future investigations of kinesins as targets for novel fungicides.
External linksJ Struct Biol / PubMed:31288039 / PubMed Central
MethodsEM (single particle)
Resolution4.5 - 5.1 Å
Structure data

3529

5mm4

EMDB-3529, PDB-5mm4:
Ustilago maydis kinesin-5 motor domain in the AMPPNP state bound to microtubules
Method: EM (single particle) / Resolution: 4.5 Å

3530

5mm7

EMDB-3530, PDB-5mm7:
Ustilago maydis kinesin-5 motor domain with N-terminal extension in the AMPPNP state bound to microtubules
Method: EM (single particle) / Resolution: 5.1 Å

Chemicals

ChemComp-MG:
Unknown entry

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

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

ChemComp-TA1:
TAXOL / medication, chemotherapy*YM

ChemComp-GDP:
GUANOSINE-5'-DIPHOSPHATE / GDP, energy-carrying molecule*YM

Source
  • ustilago maydis (strain 521 / fgsc 9021) (fungus)
  • sus scrofa (pig)
  • ustilago maydis (fungus)
KeywordsMOTOR PROTEIN / Ustilago maydis / kinesin-5

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