› 6f9w

X-ray diffraction
2.62Å resolution

Crystal structure of the LSM domain of LSM14 in complex with a C-terminal peptide of 4E-T

Released:
DOI: 10.2210/pdb6f9w/pdb
PDB entry 6f9w coloured by chain, front view.
PDB entry 6f9w coloured by chain, side view.
PDB entry 6f9w coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Molecular architecture of LSM14 interactions involved in the assembly of mRNA silencing complexes.
Brandmann T, Fakim H, Padamsi Z, Youn JY, Gingras AC, Fabian MR, Jinek M
EMBO J 37 (2018)
PMID: 29510985

Function and Biology Details

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

Structure analysis Details

Assembly composition:
hetero tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-185495 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Protein LSM14 homolog A Chain: A
Molecule details ›
Chain: A
Length: 87 amino acids
Theoretical weight: 9.67 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q8ND56 (Residues: 1-84; Coverage: 18%)
Gene names: C19orf13, FAM61A, LSM14A, RAP55, RAP55A
Sequence domains: Scd6-like Sm domain
Structure domains: SH3 type barrels.
Eukaryotic translation initiation factor 4E transporter Chain: B
Molecule details ›
Chain: B
Length: 37 amino acids
Theoretical weight: 4.14 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q9NRA8 (Residues: 954-985; Coverage: 3%)
Gene name: EIF4ENIF1

Ligands and Environments

No bound ligands
1 modified residue:
Ligand MSE 2 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X06DA
Spacegroup: P4212
Unit cell:
a: 64.89Å b: 64.89Å c: 61.67Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.222 0.22 0.245
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

5 review citations

Suppressor of clathrin deficiency (Scd6)-An emerging RGG-motif translation repressor.
Roy et al. (2018)
4 more

2 mentions without citation

Control of the eIF4E activity: structural insights and pharmacological implications.
Romagnoli et al. (2021)
1 more