The Origin of Minus-end Directionality and Mechanochemistry of Ncd Motors
Figure 1
Structural comparison of kinesin-1 and Ncd.
(a) Dimer structures of kinesin-1 (PDB ID 3KIN) in ADP-ADP state in the absence of MT. (b) Dimer structure of the symmetric Ncd dimer (PDB ID 1CZ7). Note that the Ncd motor lacks the neck-linker region. (c) Superposition of the MHs of kinesin-1 (red) and Ncd (blue). Between the MHs of the two motors Cα-rmsd is 1.06 Å, and there is 41% sequence identify. (d) Native contact maps of the two motors, upper left for Ncd and lower right for kinesin-1. Note that the patterns of the contact map between the two MH domains enclosed in black box are very similar, and that the differences are in structural motifs peripheral to MH.