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1Kinesin (dimeric) from rattus norvegicus

F. Kozielski,S. Sack,A. Marx,M. Thormahlen,E. Schonbrunn,V. Biou,A. Thompson, E.-M. Mandelkow,E. Mandelkow

1998

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2X-ray structures of monomeric and dimeric kinesin: Quaternary structure, rotational symmetry, and hinges.

S Sack,J Muller,F Kozielski,A Marx,M Thormahlen,V Biou,A Thompson,EM Mandelkow,S Brady, R Mandelkow

1997MOLECULAR BIOLOGY OF THE CELL（1997）

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3The Crystal Structure of Dimeric Kinesin and Implications for Microtubule-Dependent Motility.

F Kozielski,S Sack,A Marx,M Thormahlen,E Schonbrunn,V Biou,A Thompson,EM Mandelkow,E Mandelkow

The dimeric form of the kinesin motor and neck domain from rat brain with bound ADP has been solved by X-ray crystallography. The two heads of the dimer are connected via a coiled–coil α-helical interaction of their necks. They are broadly similar to one another; differences are most apparent in the head–neck junction and in a moderate reorientation of the neck helices in order to adopt to the coiled–coil conformation. The heads show a rotational symmetry (∼120°) about an axis close to that of the coiled–coil. This arrangement is unexpected since it is not compatible with the microtubule lattice. In this arrangement, the two heads of a kinesin dimer could not have equivalent interactions with microtubules.

1997Cell（1997）引用：528

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4Structural Studies of the Motor Protein Kinesin by Image Reconstruction and X-Ray Crystallography.

E. Mandelkow,F. Kozielski,A. Marx,E. Schonbrunn,S. Sack,V. Biou,A. Thompson, M. Thornahlen,E-M Mandelkow

Kinesin, a microtubule-activated ATPase, is a cytoplasmic motor which moves vesicles or organelles towards the distal end of microtubules.We have expressed several fragments of kinesin head domain in E. coli and used it for structural and biochemical studies of the microtubule-kinesin interaction.Open questions include: (a) Which tubulin subunit binds to kinesin?(b) What is the stoichiometry of binding?(c) How does the decoration by kinesin reveal the underlying microtubule lattice?(d) What is the polmity of the kinesin binding, and that of the tubulin subunits in a microtubule?Stmctural questions were addressed by image reconstmction of opened up microtubule walls decorated with several kinesin constructs, and by X-ray crystallography of the kinesin head domain.The reconstructions of the decorated and two-dimensionally ordered "tubulo-kinesin-complex" yields a low resolution (2nm) picture of how kinesin and Wbulin interact with one another, including the tubulinlattice, binding stoichiometry, and polarity.Altematively, the kinesin head can be induced to form wellordered 3-dimensional crystals suitable for X-ray crystallography.The solution of the structure makes use of single isomorphous replacement including anomalous diffraction at different wavelengths, using a mercury derivative of kinesin.In addition, MAD data were obtained from de1ivatives in which methionines were replaced by seleno-methionines.The interpretation of the electron density will be presented.

1996ACTA CRYSTALLOGRAPHICA A-FOUNDATION AND ADVANCES（1996）引用：23

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