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PDBsum entry 3jro
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Transport protein, structural protein
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PDB id
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3jro
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References listed in PDB file
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Key reference
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Title
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Molecular architecture of the nup84-Nup145c-Sec13 edge element in the nuclear pore complex lattice.
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Authors
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S.G.Brohawn,
T.U.Schwartz.
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Ref.
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Nat Struct Biol, 2009,
16,
1173-1177.
[DOI no: ]
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PubMed id
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Abstract
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Nuclear pore complexes (NPCs) facilitate all nucleocytoplasmic transport. These
massive protein assemblies are modular, with a stable structural scaffold
supporting more dynamically attached components. The scaffold is made from
multiple copies of the heptameric Y complex and the heteromeric Nic96 complex.
We previously showed that members of these core subcomplexes specifically share
an ACE1 fold with Sec31 of the COPII vesicle coat, and we proposed a lattice
model for the NPC based on this commonality. Here we present the crystal
structure of the heterotrimeric 134-kDa complex of Nup84-Nup145C-Sec13 of the Y
complex. The heterotypic ACE1 interaction of Nup84 and Nup145C is analogous to
the homotypic ACE1 interaction of Sec31 that forms COPII lattice edge elements
and is inconsistent with the alternative 'fence-like' NPC model. We construct a
molecular model of the Y complex and compare the architectural principles of
COPII and NPC lattices.
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Figure 2.
(a) ACE1 crown-crown interaction between Nup145C and Nup84.
(b) The same interaction between two Sec31 molecules (PDB 2PM6;
ref. 36). The Sec31 interaction is shown without domain
swapping, and the rest of the molecules are removed for clarity
(see Results). Analogous juxtaposition of crown helices  6,
7
and 8
is observed in both a and b.
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Figure 4.
A composite atomic model for the Y complex of the NPC,
emphasizing the role of the Nup84–Nup145C edge element as a
membrane curvature–stabilizing unit analogous to the
Sec31–Sec31 edge element in COPII vesicle coats. The long arm
of the Y complex is a composite model from crystal structures
and is shown with Nup145C in blue, Sec13 in orange, Nup84 in
green and Nup133 in yellow. The relative position of the
N-terminal propeller of Nup133 (yellow) and the short arm
components Nup120 (blue) and Nup85–Seh1 (blue–orange) are
more tentatively placed and shown half-transparent (see Results
for details). The long axis of the Y complex is oriented along
the positively curved nuclear envelope membrane, with the
concave face of the Nup84–Nup145C edge element facing the
lipid bilayer. This orientation is analogous to that of the
Sec31–Sec31 edge element in the COPII coat and is consistent
with the evolutionary relationship between the NPC and COPII
vesicle coat lattices. Notably, although the Y complex is shown
facing the membrane, it is not predicted to directly contact the
nuclear envelope. Rather, other nucleoporins are predicted to
have roles that correspond to adaptor complexes in other vesicle
coating systems that link the membrane curvature–stabilizing
coat (the Y complex) to the nuclear envelope.
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The above figures are
reprinted
by permission from Macmillan Publishers Ltd:
Nat Struct Biol
(2009,
16,
1173-1177)
copyright 2009.
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