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PDBsum entry 3zjy
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169 a.a.
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908 a.a.
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74 a.a.
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825 a.a.
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PDB id:
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Translation
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Title:
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Crystal structure of importin 13 - rangtp - eif1a complex
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Structure:
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Gtp-binding nuclear protein ran. Chain: a, d, f. Fragment: residues 1-180. Synonym: androgen receptor-associated protein 24, gtpase ran, ras- like protein tc4, ras-related nuclear protein. Engineered: yes. Mutation: yes. Importin-13. Chain: b, e, g.
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Source:
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Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli. Expression_system_taxid: 562. Expression_system_taxid: 562
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Resolution:
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3.60Å
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R-factor:
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0.258
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R-free:
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0.288
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Authors:
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M.Gruenwald,D.Lazzaretti,F.Bono
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Key ref:
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M.Grünwald
et al.
(2013).
Structural basis for the nuclear export activity of Importin13.
Embo J,
32,
899-913.
PubMed id:
DOI:
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Date:
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21-Jan-13
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Release date:
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10-Apr-13
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PROCHECK
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Headers
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References
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P62826
(RAN_HUMAN) -
GTP-binding nuclear protein Ran from Homo sapiens
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Seq: Struc:
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216 a.a.
169 a.a.*
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O94829
(IPO13_HUMAN) -
Importin-13 from Homo sapiens
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Seq: Struc:
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963 a.a.
908 a.a.
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Enzyme class 1:
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Chains A, D, F:
E.C.3.6.5.-
- ?????
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Enzyme class 2:
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Chains B, C, E, G:
E.C.?
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Note, where more than one E.C. class is given (as above), each may
correspond to a different protein domain or, in the case of polyprotein
precursors, to a different mature protein.
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DOI no:
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Embo J
32:899-913
(2013)
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PubMed id:
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Structural basis for the nuclear export activity of Importin13.
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M.Grünwald,
D.Lazzaretti,
F.Bono.
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ABSTRACT
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Importin13 (Imp13) is a bidirectional karyopherin that can mediate both import
and export of cargoes. Imp13 recognizes several import cargoes, which include
the exon junction complex components Mago-Y14 and the E2 SUMO-conjugating enzyme
Ubc9, and one known export cargo, the translation initiation factor 1A (eIF1A).
To understand how Imp13 can perform double duty, we determined the 3.6-Å
crystal structure of Imp13 in complex with RanGTP and with eIF1A. eIF1A binds at
the inner surface of the Imp13 C-terminal arch adjacent and concomitantly to
RanGTP illustrating how eIF1A can be exported by Imp13. Moreover, the 3.0-Å
structure of Imp13 in its unbound state reveals the existence of an open
conformation in the cytoplasm that explains export cargo release and completes
the export branch of the Imp13 pathway. Finally, we demonstrate that Imp13 is
able to bind and export eIF1A in vivo and that its function is essential.
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');
}
}
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