PDBsum entry 4gq1

Transport protein

PDB id: 4gq1

Contents

Protein chain

347 a.a.

Ligands

SO4 ×2

Waters ×81

PDB id:

4gq1

Name:

Transport protein

Title:

Nup37 of s. Pombe

Structure:

Nup37. Chain: a. Synonym: wd repeat-containing protein c4f10.18. Engineered: yes

Source:

Schizosaccharomyces pombe. Fission yeast. Organism_taxid: 4896. Gene: nup37, spac4f10.18. Expressed in: spodoptera frugiperda. Expression_system_taxid: 7108.

Resolution:

2.40Å R-factor: 0.185 R-free: 0.205

Authors:

X.Liu,J.Mitchell,R.Wozniak,G.Blobel,J.Fan

Key ref:

X.Liu et al. (2012). Structural evolution of the membrane-coating module of the nuclear pore complex. Proc Natl Acad Sci U S A, 109, 16498-16503. PubMed id: 23019579

Date:

22-Aug-12 Release date: 03-Oct-12

Protein chain

O36030  (YEKI_SCHPO) -  Uncharacterized WD repeat-containing protein C4F10.18 from Schizosaccharomyces pombe (strain 972 / ATCC 24843)

Seq: 391 a.a.

Struc: 347 a.a.

Enzyme reactions

• Enzyme class: E.C.?

Proc Natl Acad Sci U S A 109:16498-16503 (2012)

PubMed id: 23019579

Structural evolution of the membrane-coating module of the nuclear pore complex.

X.Liu, J.M.Mitchell, R.W.Wozniak, G.Blobel, J.Fan.

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.