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PDBsum entry 4wpx
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Contents |
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171 a.a.
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81 a.a.
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108 a.a.
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117 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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Structural characterization of the chaetomium thermophilum trex-2 complex and its interaction with the mRNA nuclear export factor mex67:mtr2.
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Authors
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L.Dimitrova,
E.Valkov,
S.Aibara,
D.Flemming,
S.H.Mclaughlin,
E.Hurt,
M.Stewart.
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Ref.
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Structure, 2015,
23,
1246-1257.
[DOI no: ]
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PubMed id
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Abstract
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The TREX-2 complex integrates mRNA nuclear export into the gene expression
pathway and is based on a Sac3 scaffold to which Thp1, Sem1, Sus1, and Cdc31
bind. TREX-2 also binds the mRNA nuclear export factor, Mex67:Mtr2, through the
Sac3 N-terminal region (Sac3N). Here, we characterize Chaetomium thermophilum
TREX-2, show that the in vitro reconstituted complex has an annular structure,
and define the structural basis for interactions between Sac3, Sus1, Cdc31, and
Mex67:Mtr2. Crystal structures show that the binding of C. thermophilum Sac3N
to the Mex67 NTF2-like domain (Mex67(NTF2L)) is mediated primarily through
phenylalanine residues present in a series of repeating sequence motifs that
resemble those seen in many nucleoporins, and Mlp1 also binds Mex67:Mtr2 using a
similar motif. Deletion of Sac3N generated growth and mRNA export defects in
Saccharomyces cerevisiae, and we propose TREX-2 and Mlp1 function to facilitate
export by concentrating mature messenger ribonucleoparticles at the nuclear pore
entrance.
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