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PDBsum entry 6b4j
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Transport protein
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PDB id
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6b4j
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Contents |
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315 a.a.
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44 a.a.
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38 a.a.
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426 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 and functional analysis of mRNA export regulation by the nuclear pore complex.
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Authors
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D.H.Lin,
A.R.Correia,
S.W.Cai,
F.M.Huber,
C.A.Jette,
A.Hoelz.
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Ref.
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Nat Commun, 2018,
9,
2319.
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PubMed id
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Abstract
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The nuclear pore complex (NPC) controls the passage of macromolecules between
the nucleus and cytoplasm, but how the NPC directly participates in
macromolecular transport remains poorly understood. In the final step of mRNA
export, the DEAD-box helicase DDX19 is activated by the nucleoporins Gle1,
Nup214, and Nup42 to remove Nxf1•Nxt1 from mRNAs. Here, we report crystal
structures of Gle1•Nup42 from three organisms that reveal an evolutionarily
conserved binding mode. Biochemical reconstitution of the DDX19 ATPase cycle
establishes that human DDX19 activation does not require IP6, unlike
its fungal homologs, and that Gle1 stability affects DDX19 activation. Mutations
linked to motor neuron diseases cause decreased Gle1 thermostability,
implicating nucleoporin misfolding as a disease determinant. Crystal structures
of human Gle1•Nup42•DDX19 reveal the structural rearrangements in DDX19 from
an auto-inhibited to an RNA-binding competent state. Together, our results
provide the foundation for further mechanistic analyses of mRNA export in humans.
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