› 4mml

X-ray diffraction
1.8Å resolution

D40A Hfq from Pseudomonas aeruginosa

Released:
DOI: 10.2210/pdb4mml/pdb
PDB entry 4mml coloured by chain, front view.
PDB entry 4mml coloured by chain, side view.
PDB entry 4mml coloured by chain, top view.
Source organism: Pseudomonas aeruginosa PAO1
Primary publication:
Effect of conserved intersubunit amino acid substitutions on Hfq protein structure and stability.
Murina VN, Melnik BS, Filimonov VV, Uhlein M, Weiss MS, Müller U, Nikulin AD
Biochemistry (Mosc) 79 469-77 (2014)
PMID: 24954598

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo hexamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-190968 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
RNA-binding protein Hfq Chain: A
Molecule details ›
Chain: A
Length: 82 amino acids
Theoretical weight: 9.07 KDa
Source organism: Pseudomonas aeruginosa PAO1
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q9HUM0 (Residues: 1-82; Coverage: 100%)
Gene names: PA4944, hfq
Sequence domains: Hfq protein
Structure domains: SH3 type barrels.

Ligands and Environments

3 bound ligands:
Ligand SO4 1 x SO4
Ligand MG 1 x MG
Ligand U 1 x U
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: BESSY BEAMLINE 14.1
Spacegroup: P6
Unit cell:
a: 65.79Å b: 65.79Å c: 28.13Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.172 0.164 0.203
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

6 citation in other articles

Interplay between the catabolite repression control protein Crc, Hfq and RNA in Hfq-dependent translational regulation in Pseudomonas aeruginosa.
Sonnleitner et al. (2018)
5 more

2 mentions without citation

Encoding and Multiplexing Information Signals in Magnetic Multilayers with Fractional Skyrmion Tubes.
Chen et al. (2023)
1 more