› 5dis

X-ray diffraction
2.85Å resolution

Crystal structure of a CRM1-RanGTP-SPN1 export complex bound to a 113 amino acid FG-repeat containing fragment of Nup214

Released:
DOI: 10.2210/pdb5dis/pdb
PDB entry 5dis coloured by chain, front view.
PDB entry 5dis coloured by chain, side view.
PDB entry 5dis coloured by chain, top view.
Source organisms:
Primary publication:
Structural and Functional Characterization of CRM1-Nup214 Interactions Reveals Multiple FG-Binding Sites Involved in Nuclear Export.
Port SA, Monecke T, Dickmanns A, Spillner C, Hofele R, Urlaub H, Ficner R, Kehlenbach RH
Cell Rep 13 690-702 (2015)
PMID: 26489467

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
hetero tetramer (preferred)
PDBe Complex ID:
PDB-CPX-127257 (preferred)
Entry contents:
4 distinct polypeptide molecules
Macromolecules (5 distinct):
Exportin-1 Chain: A
Molecule details ›
Chain: A
Length: 1044 amino acids
Theoretical weight: 120.4 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: O14980 (Residues: 5-1048; Coverage: 98%)
Gene names: CRM1, XPO1
Sequence domains:
GTP-binding nuclear protein Ran Chain: B
Molecule details ›
Chain: B
Length: 172 amino acids
Theoretical weight: 19.81 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P62826 (Residues: 8-179; Coverage: 80%)
Gene names: ARA24, OK/SW-cl.81, RAN
Sequence domains: Ras family
Structure domains: P-loop containing nucleotide triphosphate hydrolases
Snurportin-1 Chain: C
Molecule details ›
Chain: C
Length: 289 amino acids
Theoretical weight: 33.28 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: O95149 (Residues: 1-287; Coverage: 80%)
Gene names: RNUT1, SNUPN, SPN1
Sequence domains: Snurportin1
Structure domains: DNA ligase/mRNA capping enzyme
Maltose/maltodextrin-binding periplasmic protein; Nuclear pore complex protein Nup214 Chain: D
Molecule details ›
Chain: D
Length: 479 amino acids
Theoretical weight: 50.58 KDa
Source organisms: Expression system: Escherichia coli
UniProt:
  • Canonical: P0AEX9 (Residues: 32-387; Coverage: 96%)
  • Canonical: P35658 (Residues: 1916-2027; Coverage: 5%)
Gene names: CAIN, CAN, JW3994, KIAA0023, NUP214, b4034, malE
Sequence domains:

Ligands and Environments

Carbohydrate polymer : NEW Components: GLC
Carbohydrate polymer
3 bound ligands:
Ligand PRO 2 x PRO
Ligand GTP 1 x GTP
Ligand MG 1 x MG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: BESSY BEAMLINE 14.1
Spacegroup: C2221
Unit cell:
a: 112.33Å b: 248.97Å c: 210.57Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.208 0.206 0.249
Expression system: Escherichia coli

Quick links

Citations

6 review citations

The Multiple Faces of Disordered Nucleoporins.
Lemke EA. (2016)
5 more

7 mentions without citation

The Structure of the Nuclear Pore Complex (An Update).
Lin et al. (2019)
6 more