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Table 1.

Cryo-EM images of motor domains bound to microtubules and related structural data

Kinesin structure	ADP state	Empty state	AMPPNP/ATP-like state	References
Minus-end-directed monomer	Kar3 NTP pocket `half-open'; switch II helix α4 fairly long.	Kar3 NTP pocket wide open; α4 melted on to MT together with L11 and L12; L7 loop closer to MT, β-sheet distorted by tight binding.	Kar3 NTP pocket closed; α4 partially reformed.	Hirose et al., 2006 ^¹
Minus-end-directed dimer	Ncd second head `tethered'.	Ncd second head `tethered'.	Ncd second head `tethered'.	Hirose et al., 1998^,^⁴; Sosa et al., 1997; Wendt et al., 2002; Endres et al., 2006^,^⁵; Sablin et al., 1998^,^¹²; Kozielski et al., 1999^,^¹³; Yun et al., 2003 ^¹⁴
	Neck docked.	Neck docked or undocked.	Neck undocked.
Plus-end-directed monomer	Kif1a NTP pocket `open'; α4 in `down' position; C-terminal neck undocked; α4 extended into L11, weakening its interaction with MT.	Conventional kinesin switch II helix α4 extended into L11; weak interaction with MT — but see text.	Kif1a NTP pocket closed; α4 short and rotated to `up' position; core domain rotated relative to MT; L11 interacts with MT; C-terminal neck docked.	Kikkawa and Hirokawa, 2006^,^²; Sindelar and Downing, 2007^,^³; Rice et al., 1999^,^⁶; Neumann et al., 2006^,^⁷; Al-Bassam et al., 2003^,^⁸; Kikkawa et al., 2001; Nitta et al., 2004 ^¹⁵
		Kinesin neck undocked.
	Labelled kinesin neck undocked.		Cenp-E and Unc104 neck linkers docked, little or no rotation of core domains.
			Kinesin neck docked.
Plus-end-directed dimer	Two kinesin heads interact weakly	Kinesin second head parked firmly on first head.	Kinesin second head tethered but fairly free.	Hirose et al., 1996; Hirose et al., 1999; Cross et al., 2000^,^⁹; Arnal and Wade, 1998^,^¹⁰; Fig. 4C within Hoenger et al., 1998^,^¹¹; Kozielski et al., 1997 ^¹⁶

Kinesin structure	ADP state	Empty state	AMPPNP/ATP-like state	References
Minus-end-directed monomer	Kar3 NTP pocket `half-open'; switch II helix α4 fairly long.	Kar3 NTP pocket wide open; α4 melted on to MT together with L11 and L12; L7 loop closer to MT, β-sheet distorted by tight binding.	Kar3 NTP pocket closed; α4 partially reformed.	Hirose et al., 2006 ^¹
Minus-end-directed dimer	Ncd second head `tethered'.	Ncd second head `tethered'.	Ncd second head `tethered'.	Hirose et al., 1998^,^⁴; Sosa et al., 1997; Wendt et al., 2002; Endres et al., 2006^,^⁵; Sablin et al., 1998^,^¹²; Kozielski et al., 1999^,^¹³; Yun et al., 2003 ^¹⁴
	Neck docked.	Neck docked or undocked.	Neck undocked.
Plus-end-directed monomer	Kif1a NTP pocket `open'; α4 in `down' position; C-terminal neck undocked; α4 extended into L11, weakening its interaction with MT.	Conventional kinesin switch II helix α4 extended into L11; weak interaction with MT — but see text.	Kif1a NTP pocket closed; α4 short and rotated to `up' position; core domain rotated relative to MT; L11 interacts with MT; C-terminal neck docked.	Kikkawa and Hirokawa, 2006^,^²; Sindelar and Downing, 2007^,^³; Rice et al., 1999^,^⁶; Neumann et al., 2006^,^⁷; Al-Bassam et al., 2003^,^⁸; Kikkawa et al., 2001; Nitta et al., 2004 ^¹⁵
		Kinesin neck undocked.
	Labelled kinesin neck undocked.		Cenp-E and Unc104 neck linkers docked, little or no rotation of core domains.
			Kinesin neck docked.
Plus-end-directed dimer	Two kinesin heads interact weakly	Kinesin second head parked firmly on first head.	Kinesin second head tethered but fairly free.	Hirose et al., 1996; Hirose et al., 1999; Cross et al., 2000^,^⁹; Arnal and Wade, 1998^,^¹⁰; Fig. 4C within Hoenger et al., 1998^,^¹¹; Kozielski et al., 1997 ^¹⁶

1-3

References referring to high-resolution EM structures; ^4-11references referring to lower-resolution structures; ^12-16references referring to crystal structures.

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