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PDBsum entry 3mmy
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Nuclear protein
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PDB id
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3mmy
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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 the interaction between the nucleoporin nup98 and the mRNA export factor rae1.
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Authors
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Y.Ren,
H.S.Seo,
G.Blobel,
A.Hoelz.
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Ref.
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Proc Natl Acad Sci U S A, 2010,
107,
10406-10411.
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PubMed id
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Abstract
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The export of mRNAs is a multistep process, involving the packaging of mRNAs
into messenger ribonucleoprotein particles (mRNPs), their transport through
nuclear pore complexes, and mRNP remodeling events prior to translation.
Ribonucleic acid export 1 (Rae1) and Nup98 are evolutionarily conserved mRNA
export factors that are targeted by the vesicular stomatitis virus matrix
protein to inhibit host cell nuclear export. Here, we present the crystal
structure of human Rae1 in complex with the Gle2-binding sequence (GLEBS) of
Nup98 at 1.65 A resolution. Rae1 forms a seven-bladed beta-propeller with
several extensive surface loops. The Nup98 GLEBS motif forms an approximately
50-A-long hairpin that binds with its C-terminal arm to an essentially invariant
hydrophobic surface that extends over the entire top face of the Rae1
beta-propeller. The C-terminal arm of the GLEBS hairpin is necessary and
sufficient for Rae1 binding, and we identify a tandem glutamate element in this
arm as critical for complex formation. The Rae1*Nup98(GLEBS) surface features an
additional conserved patch with a positive electrostatic potential, and we
demonstrate that the complex possesses single-stranded RNA-binding capability.
Together, these data suggest that the Rae1*Nup98 complex directly binds to the
mRNP at several stages of the mRNA export pathway.
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