Crystal Structure of the Motor Domain of Kinesin from Rattus norvegicus

Crystal Structure of the Motor Domain of Kinesin from Rattus norvegicus




The structure of the motor domain of kinesin from Rattus norvegicus has been
solved using X-ray crystallography. The resolution of the data extends to
1.9 &Aring. The structure of the motor domain is strikingly similar to those of kinesin from Homo sapiens
(KHC)
and the minus end directed motors
Ncd and
Kar3.
The model consists of a central, eight-stranded beta-sheet with
three alpha-helices on either side. An important additional
feature in the structure of monomeric kinesin from rat is the
beginning of the C-terminal (coiled-coil in the dimer structure)
helix alpha7. The orientation of this
structural element gives hints with respect to the motility models that are
discussed in the literature.

The colour code used in the figure below corresponds to the different functional parts of the molecule: nucleotide binding regions, microtubule binding region and
neck helix alpha7. Coloured in cyan are the
central beta-sheet and in magenta the
attached helices.

We have retained the nomenclature for structural elements introduced for kinesin and Ncd. Besides the
helix alpha7 there are three more beta-strands visible in the structure of monomeric kinesin from Rattus Norvegicus: an additional anti-parallel beta-sheet formed by the N-terminal beta-0 and the C-terminal beta-9 and a strand beta-10 that forms contacts with the central beta-sheet.


Contributed by Stefan Sack & Eckhard Mandelkow

Reference
S. Sack, J. M�ller, A. Marx, M. Thorm�hlen,
E.-M. Mandelkow, S.T. Brady, and E. Mandelkow (1997)
X-ray structure of motor and neck somains of rat
brain kinesin. Biochemistry 36:16155-16165.

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Created 1 August 1998

Modified 21 February 2000 21:30 GMT