Three-dimensional structure of a tubulin-motor-protein complex

Abstract

The kinesin superfamily is a class of microtubule-based mechano-enzymes involved in intracellular transport and chromosome movements. Molecules that move towards either the plus end or the minus end of microtubules are represented within the family. The motor domains of these molecules exhibit considerable sequence homology and contain both the ATP- and microtubule-binding sites (reviewed in refs 1, 2). Here we focus on non-claret disjunctional (ncd), a minus-end-directed motor involved in chromosome segregation in meiosis and early mitosis in Drosophila. We have calculated a three-dimensional map of tubulin sheets decorated with monomeric recombinant ncd motor domains by negative-stain electron microscopy and image analysis. Comparisons with a control structure of tubulin alone reveal that each motor domain binds to the crest of a single protofilament, making extensive contacts with both the alpha and beta tubulin monomers. Binding of the motor domain results in significant conformational changes in both of the tubulin monomers.