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Structure paper

TitleThe divergent mitotic kinesin MKLP2 exhibits atypical structure and mechanochemistry.
Journal, issue, pagesElife, Vol. 6, Year 2017
Publish dateAug 11, 2017
AuthorsJoseph Atherton / I-Mei Yu / Alexander Cook / Joseph M Muretta / Agnel Joseph / Jennifer Major / Yannick Sourigues / Jeffrey Clause / Maya Topf / Steven S Rosenfeld / Anne Houdusse / Carolyn A Moores /
PubMed AbstractMKLP2, a kinesin-6, has critical roles during the metaphase-anaphase transition and cytokinesis. Its motor domain contains conserved nucleotide binding motifs, but is divergent in sequence (~35% ...MKLP2, a kinesin-6, has critical roles during the metaphase-anaphase transition and cytokinesis. Its motor domain contains conserved nucleotide binding motifs, but is divergent in sequence (~35% identity) and size (~40% larger) compared to other kinesins. Using cryo-electron microscopy and biophysical assays, we have undertaken a mechanochemical dissection of the microtubule-bound MKLP2 motor domain during its ATPase cycle, and show that many facets of its mechanism are distinct from other kinesins. While the MKLP2 neck-linker is directed towards the microtubule plus-end in an ATP-like state, it does not fully dock along the motor domain. Furthermore, the footprint of the MKLP2 motor domain on the MT surface is altered compared to motile kinesins, and enhanced by kinesin-6-specific sequences. The conformation of the highly extended loop6 insertion characteristic of kinesin-6s is nucleotide-independent and does not contact the MT surface. Our results emphasize the role of family-specific insertions in modulating kinesin motor function.
External linksElife / PubMed:28826477 / PubMed Central
MethodsEM (single particle)
Resolution4.4 - 7.9 Å
Structure data

EMDB-3620, PDB-5nd2:
Microtubule-bound MKLP2 motor domain in the presence of ADP
Method: EM (single particle) / Resolution: 5.8 Å

EMDB-3621, PDB-5nd3:
Microtubule-bound MKLP2 motor domain in the with no nucleotide
Method: EM (single particle) / Resolution: 6.1 Å

EMDB-3622, PDB-5nd4:
Microtubule-bound MKLP2 motor domain in the presence of ADP.AlFx
Method: EM (single particle) / Resolution: 4.4 Å

EMDB-3623, PDB-5nd7:
Microtubule-bound MKLP2 motor domain in the presence of AMPPNP
Method: EM (single particle) / Resolution: 7.9 Å

Chemicals

ChemComp-ADP:
ADENOSINE-5'-DIPHOSPHATE / ADP, energy-carrying molecule*YM

ChemComp-MG:
Unknown entry

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

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

ChemComp-TA1:
TAXOL / medication, chemotherapy*YM

ChemComp-ALF:
TETRAFLUOROALUMINATE ION

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

Source
  • mus musculus (house mouse)
  • bos taurus (cattle)
  • Bovine (cattle)
KeywordsMOTOR PROTEIN / Kinesin Mitosis Microtubules / Kinesin / Mitosis / Microtubules

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