› 1fo1

X-ray diffraction
2.9Å resolution

CRYSTAL STRUCTURE OF THE RNA-BINDING DOMAIN OF THE MRNA EXPORT FACTOR TAP

Released:
DOI: 10.2210/pdb1fo1/pdb
PDB entry 1fo1 coloured by chain, front view.
PDB entry 1fo1 coloured by chain, side view.
PDB entry 1fo1 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
The structure of the mRNA export factor TAP reveals a cis arrangement of a non-canonical RNP domain and an LRR domain.
Liker E, Fernandez E, Izaurralde E, Conti E
EMBO J 19 5587-98 (2000)
PMID: 11060011

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-193682 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Nuclear RNA export factor 1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 271 amino acids
Theoretical weight: 30.72 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9UBU9 (Residues: 102-372; Coverage: 44%)
Gene names: NXF1, TAP
Sequence domains: Tap, RNA-binding
Structure domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ELETTRA BEAMLINE 5.2R
Spacegroup: P43212
Unit cell:
a: 96.354Å b: 96.354Å c: 152.227Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.25 0.25 0.278
Expression system: Escherichia coli

Quick links

Citations

16 review citations

The RNA recognition motif, a plastic RNA-binding platform to regulate post-transcriptional gene expression.
Maris et al. (2005)
15 more

4 mentions without citation

The structure of the mRNA export factor TAP reveals a cis arrangement of a non-canonical RNP domain and an LRR domain.
Liker et al. (2000)
3 more