| Literature DB >> 29539637 |
Seung Joong Kim1, Javier Fernandez-Martinez2, Ilona Nudelman2, Yi Shi3, Wenzhu Zhang3, Barak Raveh1, Thurston Herricks4, Brian D Slaughter5, Joanna A Hogan6, Paula Upla7, Ilan E Chemmama1, Riccardo Pellarin1, Ignacia Echeverria1, Manjunatha Shivaraju5, Azraa S Chaudhury2, Junjie Wang3, Rosemary Williams2, Jay R Unruh5, Charles H Greenberg1, Erica Y Jacobs3, Zhiheng Yu8, M Jason de la Cruz8, Roxana Mironska2, David L Stokes7, John D Aitchison4,9, Martin F Jarrold6, Jennifer L Gerton5, Steven J Ludtke10, Christopher W Akey11, Brian T Chait3, Andrej Sali1, Michael P Rout2.
Abstract
Nuclear pore complexes play central roles as gatekeepers of RNA and protein transport between the cytoplasm and nucleoplasm. However, their large size and dynamic nature have impeded a full structural and functional elucidation. Here we determined the structure of the entire 552-protein nuclear pore complex of the yeast Saccharomyces cerevisiae at sub-nanometre precision by satisfying a wide range of data relating to the molecular arrangement of its constituents. The nuclear pore complex incorporates sturdy diagonal columns and connector cables attached to these columns, imbuing the structure with strength and flexibility. These cables also tie together all other elements of the nuclear pore complex, including membrane-interacting regions, outer rings and RNA-processing platforms. Inwardly directed anchors create a high density of transport factor-docking Phe-Gly repeats in the central channel, organized into distinct functional units. This integrative structure enables us to rationalize the architecture, transport mechanism and evolutionary origins of the nuclear pore complex.Entities:
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Year: 2018 PMID： 29539637 PMCID： PMC6022767 DOI： 10.1038/nature26003
Source DB: PubMed Journal: Nature ISSN： 0028-0836 Impact factor: 49.962