Visualizing a new binding site of ncd-motor domain on tubulin

J Struct Biol. 1999 Dec 1;128(1):26-33. doi: 10.1006/jsbi.1999.4162.

Abstract

Ncd is a microtubule minus-end directed motor of the kinesin superfamily. Previously it has been shown that ncd and kinesin motor domains share the same major binding site on microtubules. Here we report a three-dimensional EM reconstruction of negatively stained two-dimensional Zn-induced tubulin crystal sheets (Zn-sheets) decorated with the ncd motor domain at a resolution of 16 A. This work has revealed a second specific binding site for the ncd motor domain. The motor binding site on the tubulin Zn-sheets spans both alpha and beta tubulin subunits. This binding site is located at a position different from the previously identified ncd binding site on microtubules and may play a role in motor function.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Animals
  • Binding Sites
  • Crystallography / methods
  • Drosophila
  • Drosophila Proteins*
  • Electrons
  • Kinesins / chemistry*
  • Microscopy, Electron
  • Microtubules / chemistry
  • Models, Molecular
  • Protein Conformation
  • Tubulin / chemistry*
  • Zinc / chemistry

Substances

  • Drosophila Proteins
  • Tubulin
  • ncd protein, Drosophila
  • Kinesins
  • Zinc