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PDBsum entry 1cz7
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Contractile protein
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PDB id
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1cz7
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Contents |
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* Residue conservation analysis
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References listed in PDB file
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Key reference
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Title
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The crystal structure of the minus-End-Directed microtubule motor protein ncd reveals variable dimer conformations.
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Authors
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F.Kozielski,
S.De bonis,
W.P.Burmeister,
C.Cohen-Addad,
R.H.Wade.
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Ref.
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Structure, 1999,
7,
1407-1416.
[DOI no: ]
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PubMed id
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Abstract
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BACKGROUND: The kinesin superfamily of microtubule-associated motor proteins are
important for intracellular transport and for cell division in eukaryotes.
Conventional kinesins have the motor domain at the N terminus of the heavy chain
and move towards the plus end of microtubules. The ncd protein is necessary for
chromosome segregation in meiosis. It belongs to a subfamily of kinesins that
have the motor domain at the C terminus and move towards the minus end of
microtubules. RESULTS: The crystal structure of dimeric ncd has been obtained at
2.9 A resolution from crystals with the C222(1) space group, with two
independent dimers per asymmetric unit. The motor domains in these dimers are
not related by crystallographic symmetry and the two ncd dimers have
significantly different conformations. An alpha-helical coiled coil connects,
and interacts with, the motor domains. CONCLUSIONS: The ncd protein has a very
compact structure, largely due to extended interactions of the coiled coil with
the head domains. Despite this, we find that the overall conformation of the ncd
dimer can be rotated by as much as 10 degrees away from that of the
twofold-symmetric archetypal ncd. The crystal structures of conventional kinesin
and of ncd suggest a structural rationale for the reversal of the direction of
movement in chimeric kinesins.
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Figure 1.
Figure 1. The overall fold of the ncd dimer. (a) Schematic
representation of the ncd conformation and of the polypeptide
chain with the secondary structure elements visible in the
crystal structure, following the nomenclature in [9]. The
sequence in the coiled-coil helix is shown below. (b) Stereoview
of the C[a] backbone of the Drosophila melanogaster ncd dimer 1.
Every twentieth residue and also the N termini (N) and the C
termini of the two head domains are labelled. (c) Stereoview of
the structure of dimer 1. Helices of the first head domain are
coloured in orange and b strands are in light blue. In the
second head domain, helices are in red and b strands are dark
blue. The MgADP in the active site is shown as a ball-and-stick
model. This and the following figures were prepared with the
program MOLSCRIPT [32].
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The above figure is
reprinted
by permission from Cell Press:
Structure
(1999,
7,
1407-1416)
copyright 1999.
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