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Three-dimensional structure of a tubulin-motor-protein complex
Three-dimensional structure of a tubulin-motor-protein complex.
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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.
Hoenger A, Sablin EP, Vale RD, Fletterick RJ, Milligan RA
Nature
1995-07-20 00:00
376
6537
271-4
Animals,Drosophila,Image Processing, Computer-Assisted,Protein Conformation,Recombinant Proteins,Tubulin,Recombinant Proteins,Tubulin
Department of Cell Biology, Scripps Research Institute, La Jolla, California 92037, USA
Nature
0028-0836
10.1038/376271a0
581
True
7617040
