Atomic structure of the Y complex of the nuclear pore.

Publication Type:

Journal Article


Nat Struct Mol Biol, Volume 22, Issue 5, p.425-431 (2015)


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


<p>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. </p>