› 5kw1

X-ray diffraction
2.1Å resolution

Crystal Structure of the Two Tandem RRM Domains of PUF60 Bound to a Modified AdML Pre-mRNA 3' Splice Site Analogue

Released:
DOI: 10.2210/pdb5kw1/pdb
PDB entry 5kw1 coloured by chain, front view.
PDB entry 5kw1 coloured by chain, side view.
PDB entry 5kw1 coloured by chain, top view.
Source organisms:
Primary publication:
Unraveling the mechanism of recognition of the 3' splice site of the adenovirus major late promoter intron by the alternative splicing factor PUF60.
Hsiao HT, Crichlow GV, Murphy JW, Folta-Stogniew EJ, Lolis EJ, Braddock DT
OpenAccess logo PLoS One 15 e0242725 (2020)
PMID: 33253191

Function and Biology Details

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

Structure analysis Details

Assembly composition:
hetero trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-113187 (preferred)
Entry contents:
1 distinct polypeptide molecule
1 distinct DNA/RNA hybrid molecule
Macromolecules (2 distinct):
Poly(U)-binding-splicing factor PUF60 Chains: A, B
Molecule details ›
Chains: A, B
Length: 216 amino acids
Theoretical weight: 23.41 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9UHX1 (Residues: 118-316; Coverage: 36%)
Gene names: FIR, PUF60, ROBPI, SIAHBP1
Sequence domains: RNA recognition motif
Structure domains: Alpha-Beta Plaits
DNA/RNA (30-MER) Chain: C
Molecule details ›
Chain: C
Length: 30 nucleotides
Theoretical weight: 8.86 KDa
Source organism: unidentified adenovirus
Expression system: Not provided

Ligands and Environments

1 bound ligand:
Ligand CL 1 x CL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: CHESS BEAMLINE A1
Spacegroup: P31
Unit cell:
a: 62.428Å b: 62.428Å c: 83.313Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.22 0.22 0.237
Expression systems:
  • Escherichia coli
  • Not provided

Quick links

Citations

2 citation in other articles

Structural insights into a regulatory mechanism of FIR RRM1-FUSE interaction.
Ni et al. (2023)
1 more

3 mentions without citation

Accurate de novo design of hyperstable constrained peptides.
Bhardwaj et al. (2016)
2 more