Crystal Structure of the N-Terminal Domain of Nup358/RanBP2

JOURNAL OF MOLECULAR BIOLOGY

卷:423

Article

Kassube, Susanne A.¹  Stuwe, Tobias²  Lin, Daniel H.²  Antonuk, C. Danielle²  Napetschnig, Johanna¹  Blobel, Guenter¹  Hoelz, Andre^1,2 

[1] Rockefeller Univ, Howard Hughes Med Inst, Cell Biol Lab, New York, NY 10065 USA

[2] CALTECH, Div Chem & Chem Engn, Pasadena, CA 91125 USA

关键词: X-ray crystallography;    tetratricopeptide repeat (TPR);    fluorescence localization microscopy;    nuclear pore complex (NPC);    RNA binding protein;   

DOI  :  10.1016/j.jmb.2012.08.026

来源: Elsevier

【 摘 要 】

Key steps in mRNA export are the nuclear assembly of messenger ribonucleoprotein particles (mRNPs), the translocation of mRNPs through the nuclear pore complex (NPC), and the mRNP remodeling events at the cytoplasmic side of the NPC. Nup358/RanBP2 is a constituent of the cytoplasmic filaments of the NPC specific to higher eukaryotes and provides a multitude of binding sites for the nucleocytoplasmic transport machinery. Here, we present the crystal structure of the Nup358 N-terminal domain (NTD) at 0.95 angstrom resolution. The structure reveals an alpha-helical domain that harbors three central tetratricopeptide repeats (TPRs), flanked on each side by an additional solvating amphipathic alpha helix. Overall, the NTD adopts an unusual extended conformation that lacks the characteristic peptide-binding groove observed in canonical TPR domains. Strikingly, the vast majority of the NTD surface exhibits an evolutionarily conserved, positive electrostatic potential, and we demonstrate that the NTD possesses the capability to bind single-stranded RNA in solution. Together, these data suggest that the NTD contributes to mRNP remodeling events at the cytoplasmic face of the NPC. (C) 2012 Elsevier Ltd. All rights reserved.

【 授权许可】

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