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* Residue conservation analysis
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PDB id:
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Cell cycle
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Title:
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Rotation of the stalk/neck and one head in a new crystal structure of the kinesin motor protein, ncd
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Structure:
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Claret segregational protein. Chain: a, b. Fragment: ncd. Synonym: microtubule motor protein. Engineered: yes. Mutation: yes
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Source:
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Drosophila melanogaster. Fruit fly. Organism_taxid: 7227. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.
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Biol. unit:
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Dimer (from
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Resolution:
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2.50Å
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R-factor:
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0.260
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R-free:
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0.302
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Authors:
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M.Yun,C.E.Bronner,C.-G.Park,S.-S.Cha,H.-W.Park,S.A.Endow
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Key ref:
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M.Yun
et al.
(2003).
Rotation of the stalk/neck and one head in a new crystal structure of the kinesin motor protein, Ncd.
Embo J,
22,
5382-5389.
PubMed id:
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Date:
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11-Nov-02
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Release date:
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28-Oct-03
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PROCHECK
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Headers
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References
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Embo J
22:5382-5389
(2003)
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PubMed id:
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Rotation of the stalk/neck and one head in a new crystal structure of the kinesin motor protein, Ncd.
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M.Yun,
C.E.Bronner,
C.G.Park,
S.S.Cha,
H.W.Park,
S.A.Endow.
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ABSTRACT
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Molecular motors undergo conformational changes to produce force and move along
cytoskeletal filaments. Structural changes have been detected in kinesin motors;
however, further changes are expected because previous crystal structures are in
the same or closely related conformations. We report here a 2.5 A crystal
structure of the minus-end kinesin, Ncd, with the coiled-coil stalk/neck and one
head rotated by approximately 75 degrees relative to the other head. The two
heads are asymmetrically positioned with respect to the stalk and show asymmetry
of nucleotide state: one head is fully occupied, but the other is unstably bound
to ADP. Unlike previous structures, our new atomic model can be fit into
cryoelectron microscopy density maps of the motor attached to microtubules,
where it appears to resemble a one-head-bound motor with the stalk rotated
towards the minus end. Interactions between neck and motor core residues,
observed in the head that moves with the stalk, are disrupted in the other head,
permitting rotation of the stalk/neck. The rotation could represent a
force-producing stroke that directs the motor to the minus end.
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Literature references that cite this PDB file's key reference
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PubMed id
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Reference
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N.Naber,
A.Larson,
S.Rice,
R.Cooke,
and
E.Pate
(2011).
Multiple conformations of the nucleotide site of Kinesin family motors in the triphosphate state.
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J Mol Biol,
408,
628-642.
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E.Heuston,
C.E.Bronner,
F.J.Kull,
and
S.A.Endow
(2010).
A kinesin motor in a force-producing conformation.
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BMC Struct Biol,
10,
19.
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PDB code:
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R.A.Cross
(2010).
Kinesin-14: the roots of reversal.
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BMC Biol,
8,
107.
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A.Marx,
A.Hoenger,
and
E.Mandelkow
(2009).
Structures of kinesin motor proteins.
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Cell Motil Cytoskeleton,
66,
958-966.
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E.Kocik,
K.J.Skowronek,
and
A.A.Kasprzak
(2009).
Interactions between subunits in heterodimeric Ncd molecules.
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J Biol Chem,
284,
35735-35745.
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S.Adio,
and
G.Woehlke
(2009).
Properties of the kinesin-3 NcKin3 motor domain and implications for neck function.
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FEBS J,
276,
3641-3655.
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S.Adio,
J.Jaud,
B.Ebbing,
M.Rief,
and
G.Woehlke
(2009).
Dissection of kinesin's processivity.
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PLoS ONE,
4,
e4612.
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L.A.Amos
(2008).
Molecular motors: not quite like clockwork.
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Cell Mol Life Sci,
65,
509-515.
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J.S.Allingham,
L.R.Sproul,
I.Rayment,
and
S.P.Gilbert
(2007).
Vik1 modulates microtubule-Kar3 interactions through a motor domain that lacks an active site.
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Cell,
128,
1161-1172.
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PDB code:
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L.A.Amos,
and
K.Hirose
(2007).
A cool look at the structural changes in kinesin motor domains.
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J Cell Sci,
120,
3919-3927.
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A.Marx,
J.Müller,
E.M.Mandelkow,
A.Hoenger,
and
E.Mandelkow
(2006).
Interaction of kinesin motors, microtubules, and MAPs.
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J Muscle Res Cell Motil,
27,
125-137.
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K.Hirose,
E.Akimaru,
T.Akiba,
S.A.Endow,
and
L.A.Amos
(2006).
Large conformational changes in a kinesin motor catalyzed by interaction with microtubules.
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Mol Cell,
23,
913-923.
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N.F.Endres,
C.Yoshioka,
R.A.Milligan,
and
R.D.Vale
(2006).
A lever-arm rotation drives motility of the minus-end-directed kinesin Ncd.
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Nature,
439,
875-878.
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Q.Shao,
and
Y.Q.Gao
(2006).
On the hand-over-hand mechanism of kinesin.
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Proc Natl Acad Sci U S A,
103,
8072-8077.
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S.Adio,
M.Bloemink,
M.Hartel,
S.Leier,
M.A.Geeves,
and
G.Woehlke
(2006).
Kinetic and mechanistic basis of the nonprocessive Kinesin-3 motor NcKin3.
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J Biol Chem,
281,
37782-37793.
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T.Shima,
T.Kon,
K.Imamula,
R.Ohkura,
and
K.Sutoh
(2006).
Two modes of microtubule sliding driven by cytoplasmic dynein.
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Proc Natl Acad Sci U S A,
103,
17736-17740.
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C.J.Sciambi,
D.J.Komma,
H.N.Sköld,
K.Hirose,
and
S.A.Endow
(2005).
A bidirectional kinesin motor in live Drosophila embryos.
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Traffic,
6,
1036-1046.
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H.M.Chu,
M.Yun,
D.E.Anderson,
H.Sage,
H.W.Park,
and
S.A.Endow
(2005).
Kar3 interaction with Cik1 alters motor structure and function.
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EMBO J,
24,
3214-3223.
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|
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E.P.Sablin,
and
R.J.Fletterick
(2004).
Coordination between motor domains in processive kinesins.
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J Biol Chem,
279,
15707-15710.
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|
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M.V.Vinogradova,
V.S.Reddy,
A.S.Reddy,
E.P.Sablin,
and
R.J.Fletterick
(2004).
Crystal structure of kinesin regulated by Ca(2+)-calmodulin.
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J Biol Chem,
279,
23504-23509.
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PDB code:
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T.Ogawa,
R.Nitta,
Y.Okada,
and
N.Hirokawa
(2004).
A common mechanism for microtubule destabilizers-M type kinesins stabilize curling of the protofilament using the class-specific neck and loops.
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Cell,
116,
591-602.
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PDB codes:
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L.Wordeman
(2003).
Breathing down the neck of Unc104.
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J Cell Biol,
163,
693-695.
|
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|
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The most recent references are shown first.
Citation data come partly from CiteXplore and partly
from an automated harvesting procedure. Note that this is likely to be
only a partial list as not all journals are covered by
either method. However, we are continually building up the citation data
so more and more references will be included with time.
Where a reference describes a PDB structure, the PDB
code is
shown on the right.
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}
}
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