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PDBsum entry 2f6h
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Structural protein
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PDB id
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2f6h
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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 basis for myosin V discrimination between distinct cargoes.
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Authors
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N.Pashkova,
Y.Jin,
S.Ramaswamy,
L.S.Weisman.
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Ref.
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EMBO J, 2006,
25,
693-700.
[DOI no: ]
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PubMed id
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Abstract
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Myosin V molecular motors move cargoes on actin filaments. A myosin V may move
multiple cargoes to distinct places at different times. The cargoes attach to
the globular tail of myosin V via cargo-specific receptors. Here we report the
crystal structure at 2.2 A of the myosin V globular tail. The overall tertiary
structure has not been previously observed. There are several patches of highly
conserved regions distributed on the surface of the tail. These are candidate
attachment sites for cargo-specific receptors. Indeed, we identified a region of
five conserved surface residues that are solely required for vacuole
inheritance. Likewise, we identified a region of five conserved surface residues
that are required for secretory vesicle movement, but not vacuole movement.
These two regions are at opposite ends of the oblong-shaped cargo-binding
domain, and moreover are offset by 180 degrees. The fact that the cargo-binding
areas are distant from each other and simultaneously exposed on the surface of
the globular tail suggests that major targets for the regulation of cargo
attachment are organelle-specific myosin V receptors.
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Figure 1.
Figure 1 Structural overview of the Myo2p globular tail. (A)
Ribbon representation of the structure in two orientations
(rainbow colors from blue, N-terminus, to red, C-terminus).
Vacuole-specific mutations D1297G/N, L1301P, N1304S, and
N1307D/N are indicated in magenta. The most amino-terminal
residue within the solved structure is 1152. (B) Topology
diagram. Subdomain I is blue and subdomain II is red. Cyan
indicates the region of the C-loop that is part of subdomain I.
All structures presented in the figures were drawn using PyMol
(DeLano Scientific LLC).
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Figure 5.
Figure 5 The vacuole- and secretory vesicle-binding sites are
structurally separated within the Myo2p globular tail. Surface
residues of subdomain I are shown in blue and that of subdomain
II in red. Vacuole-binding site is in cyan and secretory
vesicle-specific site is in yellow. This present figure and
Figure 3 show the same orientation.
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The above figures are
reprinted
by permission from Macmillan Publishers Ltd:
EMBO J
(2006,
25,
693-700)
copyright 2006.
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