Evidence and sources

Measurements

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Big picture numbers

Structures

• 4HNA
  Kinesin-1 head on tubulin, ATP-like

  The front half of the step: ATP-like kinesin on tubulin with the neck linker docked. It is the end state of the power stroke. X-ray diffraction, 3.19 Å.
• 4LNU
  Kinesin-1 head on tubulin, no nucleotide

  The waiting state: a tubulin-bound head with an empty nucleotide pocket. It pairs with 4HNA to show how ATP binding rotates the head subdomains. X-ray diffraction, 2.19 Å.
• 3J8X
  Kinesin-1 on a microtubule, no nucleotide

  Same construct and same lattice as 3J8Y, so the two entries form the cleanest morph of neck-linker docking on a real microtubule. Electron microscopy, 5 Å.
• 3J8Y
  Kinesin-1 on a microtubule, ATP analogue

  One kinesin head on one lattice αβ dimer in the ATP state. Copy this unit along a protofilament to decorate the microtubule. Electron microscopy, 5 Å.
• 3KIN
  Kinesin-1 dimer with neck coiled coil

  The only kinesin-1 dimer crystal structure. It gives the neck coiled coil that joins the two heads. The head arrangement does not fit the lattice, so use it for the neck, not for the stepping pose. X-ray diffraction, 3.1 Å.
• 8RHH
  Tail-locked kinesin-1 dimer on tubulin

  Shows both kinesin-1 heads to residue 346 and the tail that switches the motor off. Use it for a regulation panel, not for the walking cycle. Electron microscopy, 3 Å.
• 1JFF
  αβ-tubulin dimer

  The classic refined tubulin dimer. It is a light building block for the lattice when the kinesin-bound dimer is not needed. Electron crystallography, 3.5 Å.
• 6EVZ
  13-protofilament GDP microtubule patch

  A real 13-protofilament lattice patch. The lattice numbers in 'geometry' were measured from it. Electron microscopy, 3.8 Å.
• 6DPU
  GMPCPP microtubule patch, 3.1 Å

  The highest-resolution undecorated lattice here. It shows the longer 8.4 nm dimer repeat of the GTP-like lattice. Electron microscopy, 3.1 Å.
• 1BG2
  Human kinesin-1 head alone

  The first kinesin head structure. It revealed the shared core with myosin, so use it on the evolution panel. X-ray diffraction, 1.8 Å.
• 8UTN
  Kinesin-3 KIF1A dimer, both heads bound

  A real two-heads-bound kinesin dimer on one protofilament. It is the best template for the stepping pose, and it is the kinesin-3 swap. Electron microscopy, 3.1 Å.
• 1I5S
  Kinesin-3 KIF1A head, ADP

  ADP partner of 1I6I. Same construct, so the pair morphs the switch motion of a kinesin-3 head. X-ray diffraction, 2.2 Å.
• 1I6I
  Kinesin-3 KIF1A head, ATP analogue

  ATP-like partner of 1I5S. X-ray diffraction, 2 Å.
• 2NCD
  Kinesin-14 Ncd dimer, minus-end motor

  The minus-end swap. Its coiled-coil neck, not its motor core, sets the direction. X-ray diffraction, 2.5 Å.
• 1II6
  Kinesin-5 Eg5 head, ADP

  ADP state of the kinesin-5 swap. It shows a neck linker docked in an unusual position. X-ray diffraction, 2.1 Å.
• 3HQD
  Kinesin-5 Eg5 head, ATP analogue

  ATP-like partner of 1II6 for the kinesin-5 morph. X-ray diffraction, 2.19 Å.
• 5MIO
  Kinesin-13 MCAK bending tubulin

  The kinesin-13 swap. This motor does not walk. It holds tubulin in a curved shape and peels dimers off microtubule ends. X-ray diffraction, 3.19 Å.

References

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33. 33Walker et al., Nature 1990. The Drosophila claret segregation protein is a minus-end directed motor molecule
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