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PDBsum entry 4gq1
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Transport protein
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PDB id
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4gq1
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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 evolution of the membrane-Coating module of the nuclear pore complex.
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Authors
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X.Liu,
J.M.Mitchell,
R.W.Wozniak,
G.Blobel,
J.Fan.
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Ref.
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Proc Natl Acad Sci U S A, 2012,
109,
16498-16503.
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PubMed id
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Abstract
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The coatomer module of the nuclear pore complex borders the cylinder-like
nuclear pore-membrane domain of the nuclear envelope. In evolution, a single
coatomer module increases in size from hetero-heptamer (Saccharomyces
cerevisiae) to hetero-octamer (Schizosaccharomyces pombe) to hetero-nonamer
(Metazoa). Notably, the heptamer-octamer transition proceeds through the
acquisition of the nucleoporin Nup37. How Nup37 contacts the heptamer remained
unknown. Using recombinant nucleoporins, we show that Sp-Nup37 specifically
binds the Sp-Nup120 member of the hetero-heptamer but does not bind an Sc-Nup120
homolog. To elucidate the Nup37-Nup120 interaction at the atomic level, we
carried out crystallographic analyses of Sp-Nup37 alone and in a complex with an
N-terminal, ∼110-kDa fragment of Sp-Nup120 comprising residues 1-950.
Corroborating structural predictions, we determined that Nup37 folds into a
seven-bladed β-propeller. Several disordered surface regions of the Nup37
β-propeller assume structure when bound to Sp-Nup120. The N-terminal domain of
Sp-Nup120(1-950) also folds into a seven-bladed propeller with a markedly
protruding 6D-7A insert and is followed by a contorted helical domain.
Conspicuously, this 6D-7A insert contains an extension of 50 residues which also
is highly conserved in Metazoa but is absent in Sc-Nup120. Strikingly, numerous
contacts with the Nup37 β-propeller are located on this extension of the 6D-7A
insert. Another contact region is situated toward the end of the helical region
of Sp-Nup120(1-950). Our findings provide information about the evolution and
the assembly of the coatomer module of the nuclear pore complex.
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