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PDBsum entry 2d2s
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Endocytosis/exocytosis
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PDB id
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2d2s
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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 structures of exocyst subunit exo70p and the exo84p c-Terminal domains reveal a common motif.
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Authors
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G.Dong,
A.H.Hutagalung,
C.Fu,
P.Novick,
K.M.Reinisch.
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Ref.
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Nat Struct Mol Biol, 2005,
12,
1094-1100.
[DOI no: ]
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PubMed id
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Abstract
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The exocyst is a large complex that is required for tethering vesicles at the
final stages of the exocytic pathway in all eukaryotes. Here we present the
structures of the Exo70p subunit of this complex and of the C-terminal domains
of Exo84p, at 2.0-A and 2.85-A resolution, respectively. Exo70p forms a
160-A-long rod with a novel fold composed of contiguous alpha-helical bundles.
The Exo84p C terminus also forms a long rod (80 A), which unexpectedly has the
same fold as the Exo70p N terminus. Our structural results and our experimental
observations concerning the interaction between Exo70p and other exocyst
subunits or Rho3p GTPase are consistent with an architecture wherein exocyst
subunits are composed of mostly helical modules strung together into long rods.
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Figure 1.
Figure 1. Exo70p is a long rod composed of contiguous  -helical
bundles. (a) Ribbon diagram of Exo70p colored from blue at
its N terminus to red at its C terminus. Domains A-D are
indicated. (b) Exo70p colored according to electrostatic surface
potential (on a scale from -15 kT to +15 kT), where blue is
positive and red is negative. Exo70p is strikingly dipolar, with
the N terminus negatively and the C terminus positively charged.
The orientation on the left is as in a. Arrows indicate a
conserved patch of arginine and lysine residues at the extreme C
terminus of Exo70p (see Supplementary Fig. 2). (c) Sequence of
Exo70p. Secondary structure elements are labeled as in a;
helices that span domains are blue. Dotted lines represent
regions in the crystal structure that are disordered. This
figure was prepared using MolScript32 and GRASP
(http://trantor.bioc.columbia.edu/grasp/)33.
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Figure 5.
Figure 5. The structure of the Exo84p C terminus is similar to
that of the Exo70p N terminus. (a) Exo84p C-terminal fragment
(residues 523-753), colored from blue at residue 523 to red at
residue 753. (b)Exo84 C-terminal fragment colored according to
electrostatic surface potential (on a scale from -13 kT to +11
kT), where blue is positive and red is negative. The view on the
left is as in a. (c) Exo70p N-terminal fragment (residues
67-341). (d) A superposition of the Exo84p C terminus (blue) and
the Exo70p N terminus (pink) aligned using helices H1-H4 of
Exo84p and H1-H3 and H5 of Exo70p (circled). The two helical
bundles comprising the two protein fragments are differently
oriented in Exo84p and Exo70p. The view is as in a and c. (e) A
superposition of the Exo84p C terminus and the Exo70p N terminus
aligned using helices H5-H9 of Exo84p and H6-H10 of Exo70p
(circled). In the interest of clarity, the view is rotated with
respect to that in d. Lsqman34 was used in the alignments in d
and e. Figures were prepared with MolScript32 and GRASP33.
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The above figures are
reprinted
by permission from Macmillan Publishers Ltd:
Nat Struct Mol Biol
(2005,
12,
1094-1100)
copyright 2005.
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