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Structure paper

TitleX-ray and Cryo-EM structures reveal mutual conformational changes of Kinesin and GTP-state microtubules upon binding.
Journal, issue, pagesEMBO J, Vol. 34, Issue 9, Page 1270-1286, Year 2015
Publish dateMay 5, 2015
AuthorsManatsu Morikawa / Hiroaki Yajima / Ryo Nitta / Shigeyuki Inoue / Toshihiko Ogura / Chikara Sato / Nobutaka Hirokawa /
PubMed AbstractThe molecular motor kinesin moves along microtubules using energy from ATP hydrolysis in an initial step coupled with ADP release. In neurons, kinesin-1/KIF5C preferentially binds to the GTP-state ...The molecular motor kinesin moves along microtubules using energy from ATP hydrolysis in an initial step coupled with ADP release. In neurons, kinesin-1/KIF5C preferentially binds to the GTP-state microtubules over GDP-state microtubules to selectively enter an axon among many processes; however, because the atomic structure of nucleotide-free KIF5C is unavailable, its molecular mechanism remains unresolved. Here, the crystal structure of nucleotide-free KIF5C and the cryo-electron microscopic structure of nucleotide-free KIF5C complexed with the GTP-state microtubule are presented. The structures illustrate mutual conformational changes induced by interaction between the GTP-state microtubule and KIF5C. KIF5C acquires the 'rigor conformation', where mobile switches I and II are stabilized through L11 and the initial portion of the neck-linker, facilitating effective ADP release and the weak-to-strong transition of KIF5C microtubule affinity. Conformational changes to tubulin strengthen the longitudinal contacts of the GTP-state microtubule in a similar manner to GDP-taxol microtubules. These results and functional analyses provide the molecular mechanism of the preferential binding of KIF5C to GTP-state microtubules.
External linksEMBO J / PubMed:25777528 / PubMed Central
MethodsEM (single particle) / X-ray diffraction
Resolution2.7 - 8.1 Å
Structure data

5916

3j6h

EMDB-5916: Cryo-Electron Microscopy of Nucleotide-free Kinesin motor domain complexed with GMPCPP-microtubule
PDB-3j6h: Nucleotide-free Kinesin motor domain complexed with GMPCPP-microtubule
Method: EM (single particle) / Resolution: 8.1 Å

PDB-3wrd:
Crystal Structure of the KIF5C Motor Domain Without Any Nucleotide
Method: X-RAY DIFFRACTION / Resolution: 2.86 Å

PDB-3x2t:
Crystal Structure of the KIF5C Motor Domain With ADP
Method: X-RAY DIFFRACTION / Resolution: 2.7 Å

Chemicals

ChemComp-MG:
Unknown entry

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

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

ChemComp-SO4:
SULFATE ION / Sulfate

ChemComp-HOH:
WATER / Water

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

Source
  • sus scrofa (pig)
  • mus musculus (house mouse)
KeywordsSTRUCTURAL PROTEIN/MOTOR PROTEIN / Kinesin / Motor domain / Rigor-conformation / Nucleotide-free kinesin / Microtubule / GMPCPP-microtubule / tubulin / Axonal transport / STRUCTURAL PROTEIN-MOTOR PROTEIN complex / MOTOR PROTEIN / nucleotide-free / ATPase / nucleotide binding / transport protein

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