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PDBsum entry 3fwc
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Cell cycle, transcription
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PDB id
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3fwc
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Contents |
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145 a.a.
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83 a.a.
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87 a.a.
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92 a.a.
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78 a.a.
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References listed in PDB file
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Key reference
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Title
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Sus1, Cdc31, And the sac3 cid region form a conserved interaction platform that promotes nuclear pore association and mRNA export.
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Authors
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D.Jani,
S.Lutz,
N.J.Marshall,
T.Fischer,
A.Köhler,
A.M.Ellisdon,
E.Hurt,
M.Stewart.
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Ref.
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Mol Cell, 2009,
33,
727-737.
[DOI no: ]
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PubMed id
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Abstract
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The yeast Sac3:Cdc31:Sus1:Thp1 (TREX-2) complex facilitates the repositioning
and association of actively transcribing genes with nuclear pores (NPCs)-"gene
gating"-that is central to integrating transcription, processing, and mRNA
nuclear export. We present here the crystal structure of Sus1 and Cdc31 bound to
a central region of Sac3 (the CID domain) that is crucial for its function.
Sac3(CID) forms a long, gently undulating alpha helix around which one Cdc31 and
two Sus1 chains are wrapped. Sus1 has an articulated helical hairpin fold that
facilitates its wrapping around Sac3. In vivo studies using engineered mutations
that selectively disrupted binding of individual chains to Sac3 indicated that
Sus1 and Cdc31 function synergistically to promote NPC association of TREX-2 and
mRNA nuclear export. These data indicate Sac3(CID) provides a scaffold within
TREX-2 to integrate interactions between protein complexes to facilitate the
coupling of transcription and mRNA export during gene expression.
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Figure 2.
Overview of Crystal Structure of the Sac3^CID:Cdc31:Sus1
Complex (A) Surface view. (B) Secondary structure schematic.
Cdc31 is yellow, Sac3 is red, Sus1A is blue, and Sus1B is cyan.
Residues 723 --805 of Sac3 form a continuous, 12.5 nm-long,
gently undulating, [alpha] helix to which one Cdc31 and two Sus1
(Sus1A and Sus1B) chains bind. (C) Schematic of the principal
residues that are buried in the interfaces between Sac3 and its
partners. Dashed lines represent putative H bonds. Mol Cell.
2009 March 27; 33(6-2): 727–737. doi:
10.1016/j.molcel.2009.01.033. Copyright [copyright] 2009 ELL &
Excerpta Medica
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Figure 3.
Sus1:Sac3 Interaction (A and B) The hinges between the rigid
Sus1 [alpha] helices enable the molecule to wrap around the
Sac3^CID helix, shown in red. (C) End-on view showing Sus1
wrapping around the Sac3 helix like fingers gripping a rod. (D)
Sus1 sequences showing the conservation of both the helices
([alpha]1, [alpha]2, [alpha]3, [alpha]4, and [alpha]5) and the
hinges between them. Single Gly residues (yellow) form the
hinges between helices [alpha]1/[alpha]2 and [alpha]2/[alpha]3.
A kink introduced by a Pro in helix [alpha]4 enhances the
intimacy of the contact with Sac3. Mol Cell. 2009 March 27;
33(6-2): 727–737. doi: 10.1016/j.molcel.2009.01.033. Copyright
[copyright] 2009 ELL & Excerpta Medica
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The above figures are
reprinted
from an Open Access publication published by Cell Press:
Mol Cell
(2009,
33,
727-737)
copyright 2009.
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