› 4fgv

X-ray diffraction
2.94Å resolution

Crystal structure of free CRM1 (crystal form 1)

Released:
DOI: 10.2210/pdb4fgv/pdb
PDB entry 4fgv coloured by chain, front view.
PDB entry 4fgv coloured by chain, side view.
PDB entry 4fgv coloured by chain, top view.
Source organism: Thermochaetoides thermophila DSM 1495
Primary publication:
Structural basis for cooperativity of CRM1 export complex formation.
Monecke T, Haselbach D, Voß B, Russek A, Neumann P, Thomson E, Hurt E, Zachariae U, Stark H, Grubmüller H, Dickmanns A, Ficner R
Proc Natl Acad Sci U S A 110 960-5 (2013)
PMID: 23277578

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-123916 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Exportin-1 C-terminal domain-containing protein Chain: A
Molecule details ›
Chain: A
Length: 1086 amino acids
Theoretical weight: 124.64 KDa
Source organism: Thermochaetoides thermophila DSM 1495
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: G0RZB7 (Residues: 1-22, 23-46, 47-47, 48-1043; Coverage: 100%)
Gene name: CTHT_0002400
Sequence domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: BESSY BEAMLINE 14.1
Spacegroup: P212121
Unit cell:
a: 85.122Å b: 139.073Å c: 174.875Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.221 0.22 0.243
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

5 review citations

Atomic basis of CRM1-cargo recognition, release and inhibition.
Fung et al. (2014)
4 more

10 mentions without citation

Karyopherin-mediated nucleocytoplasmic transport.
Wing et al. (2022)
9 more