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.

journal_name

Nature

journal_title

Nature

authors

Hoenger A,Sablin EP,Vale RD,Fletterick RJ,Milligan RA

doi

10.1038/376271a0

subject

Has Abstract

pub_date

1995-07-20 00:00:00

pages

271-4

issue

6537

eissn

0028-0836

issn

1476-4687

journal_volume

376

pub_type

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