4GQ2

S. pombe Nup120-Nup37 complex

Summary for 4GQ2

• Entry DOI: 10.2210/pdb4gq2/pdb
• Related: 4GQ1
• Descriptor: Nucleoporin nup120, Nup37 (3 entities in total)
• Functional Keywords: beta propeller alpha helical, component of nuclear pore complex, transport protein
• Biological source: Schizosaccharomyces pombe (fission yeast); More
• Cellular location: Nucleus: O43044; Cytoplasm: O36030
• Total number of polymer chains: 2
• Total formula weight: 151295.57

Authors

Liu, X.,Mitchell, J.,Wozniak, R.,Blobel, G.,Fan, J. (deposition date: 2012-08-22, release date: 2012-10-03, Last modification date: 2023-09-13)

Primary citation

Liu, X.,Mitchell, J.M.,Wozniak, R.W.,Blobel, G.,Fan, J.
Structural evolution of the membrane-coating module of the nuclear pore complex.
Proc.Natl.Acad.Sci.USA, 109:16498-16503, 2012

PubMed Abstract: The coatomer module of the nuclear pore complex borders the cylinder-like nuclear pore-membrane domain of the nuclear envelope. In evolution, a single coatomer module increases in size from hetero-heptamer (Saccharomyces cerevisiae) to hetero-octamer (Schizosaccharomyces pombe) to hetero-nonamer (Metazoa). Notably, the heptamer-octamer transition proceeds through the acquisition of the nucleoporin Nup37. How Nup37 contacts the heptamer remained unknown. Using recombinant nucleoporins, we show that Sp-Nup37 specifically binds the Sp-Nup120 member of the hetero-heptamer but does not bind an Sc-Nup120 homolog. To elucidate the Nup37-Nup120 interaction at the atomic level, we carried out crystallographic analyses of Sp-Nup37 alone and in a complex with an N-terminal, ~110-kDa fragment of Sp-Nup120 comprising residues 1-950. Corroborating structural predictions, we determined that Nup37 folds into a seven-bladed β-propeller. Several disordered surface regions of the Nup37 β-propeller assume structure when bound to Sp-Nup120. The N-terminal domain of Sp-Nup120(1-950) also folds into a seven-bladed propeller with a markedly protruding 6D-7A insert and is followed by a contorted helical domain. Conspicuously, this 6D-7A insert contains an extension of 50 residues which also is highly conserved in Metazoa but is absent in Sc-Nup120. Strikingly, numerous contacts with the Nup37 β-propeller are located on this extension of the 6D-7A insert. Another contact region is situated toward the end of the helical region of Sp-Nup120(1-950). Our findings provide information about the evolution and the assembly of the coatomer module of the nuclear pore complex.

PubMed: 23019579
DOI: 10.1073/pnas.1214557109

Experimental method

X-RAY DIFFRACTION (2.4 Å)