Atomic structure of the Y complex of the nuclear pore

Nat Struct Mol Biol. 2015 May;22(5):425-431. doi: 10.1038/nsmb.2998. Epub 2015 Mar 30.

Abstract

The nuclear pore complex (NPC) is the principal gateway for transport into and out of the nucleus. Selectivity is achieved through the hydrogel-like core of the NPC. The structural integrity of the NPC depends on ~15 architectural proteins, which are organized in distinct subcomplexes to form the >40-MDa ring-like structure. Here we present the 4.1-Å crystal structure of a heterotetrameric core element ('hub') of the Y complex, the essential NPC building block, from Myceliophthora thermophila. Using the hub structure together with known Y-complex fragments, we built the entire ~0.5-MDa Y complex. Our data reveal that the conserved core of the Y complex has six rather than seven members. Evolutionarily distant Y-complex assemblies share a conserved core that is very similar in shape and dimension, thus suggesting that there are closely related architectural codes for constructing the NPC in all eukaryotes.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Amino Acid Sequence
  • Cell Nucleus / metabolism
  • Crystallography, X-Ray
  • Humans
  • Models, Molecular
  • Molecular Docking Simulation
  • Nuclear Pore / ultrastructure*
  • Nuclear Pore Complex Proteins / analysis*
  • Protein Structure, Tertiary
  • Saccharomyces cerevisiae / metabolism
  • Saccharomyces cerevisiae Proteins / metabolism
  • Sequence Alignment
  • Sordariales / metabolism*

Substances

  • Nuclear Pore Complex Proteins
  • Saccharomyces cerevisiae Proteins

Associated data

  • PDB/4YCZ