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PDBsum entry 2zfk
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Transport protein
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PDB id
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2zfk
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References listed in PDB file
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Key reference
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Title
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Structural model for strain-Dependent microtubule activation of mg-Adp release from kinesin.
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Authors
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R.Nitta,
Y.Okada,
N.Hirokawa.
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Ref.
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Nat Struct Biol, 2008,
15,
1067-1075.
[DOI no: ]
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PubMed id
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Note In the PDB file this reference is
annotated as "TO BE PUBLISHED".
The citation details given above were identified by an automated
search of PubMed on title and author
names, giving a
perfect match.
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Abstract
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Mg-ADP release is considered to be a crucial process for the regulation and
motility of kinesin. To gain insight into the structural basis of this process,
we solved the atomic structures of kinesin superfamily protein-1A (KIF1A) during
and after Mg(2+) release. On the basis of new structural and mutagenesis data,
we propose a model mechanism for microtubule activation of Mg-ADP release from
KIF1A. In our model, a specific interaction between loop L7 of KIF1A and
beta-tubulin reconfigures the KIF1A active site by shifting the relative
positions of switches I and II. This leads to the sequential release of a group
of water molecules that sits over the Mg(2+) in the active site, followed by
Mg(2+) and finally the ADP. We further propose that this set of events is linked
to a strain-dependent docking of the neck linker to the motor core, which
produces a two-step power stroke.
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Figure 2.
(a) Superposition (with the use of the C  atoms
of P-loop) of the five structures, K-Mg-ADP (red), transition 1
(orange), transition 2 (yellow green), transition 3 (cyan) and
K-ADP (blue) are shown, seen from the microtubule binding side.
(b) The r.m.s. deviations between the K-Mg-ADP and the K-ADP
states are indicated by the colorings: higher r.m.s. deviations
are shown in warmer colors and lower values in cooler colors.
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Figure 8.
See text for details.
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The above figures are
reprinted
by permission from Macmillan Publishers Ltd:
Nat Struct Biol
(2008,
15,
1067-1075)
copyright 2008.
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