› 3sde

X-ray diffraction
1.9Å resolution

Crystal structure of a paraspeckle-protein heterodimer, PSPC1/NONO

Released:
DOI: 10.2210/pdb3sde/pdb
PDB entry 3sde coloured by chain, front view.
PDB entry 3sde coloured by chain, side view.
PDB entry 3sde coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structure of the heterodimer of human NONO and paraspeckle protein component 1 and analysis of its role in subnuclear body formation.
Passon DM, Lee M, Rackham O, Stanley WA, Sadowska A, Filipovska A, Fox AH, Bond CS
Proc Natl Acad Sci U S A 109 4846-50 (2012)
PMID: 22416126

Function and Biology Details

Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-172235 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Paraspeckle component 1 Chain: A
Molecule details ›
Chain: A
Length: 261 amino acids
Theoretical weight: 30 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q8WXF1 (Residues: 61-320; Coverage: 50%)
Gene names: PSP1, PSPC1
Sequence domains:
Structure domains:
Non-POU domain-containing octamer-binding protein Chain: B
Molecule details ›
Chain: B
Length: 261 amino acids
Theoretical weight: 30.28 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q15233 (Residues: 53-312; Coverage: 55%)
Gene names: NONO, NRB54
Sequence domains:
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand EDO 11 x EDO
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: AUSTRALIAN SYNCHROTRON BEAMLINE MX2
Spacegroup: C2
Unit cell:
a: 90.9Å b: 67.18Å c: 94.08Å
α: 90° β: 99.96° γ: 90°
R-values:
R R work R free
0.186 0.183 0.228
Expression system: Escherichia coli

Quick links

Citations

15 review citations

Phase separation in biology; functional organization of a higher order.
Mitrea et al. (2016)
14 more

12 mentions without citation

The DBHS proteins SFPQ, NONO and PSPC1: a multipurpose molecular scaffold.
Knott et al. (2016)
11 more