› 4hqs

X-ray diffraction
1.48Å resolution

Crystal structure of the pneumoccocal exposed lipoprotein thioredoxin sp_0659 (Etrx1) from Streptococcus pneumoniae strain TIGR4

Released:
DOI: 10.2210/pdb4hqs/pdb
PDB entry 4hqs coloured by chain, front view.
PDB entry 4hqs coloured by chain, side view.
PDB entry 4hqs coloured by chain, top view.
Source organism: Streptococcus pneumoniae TIGR4
Primary publication:
Molecular architecture of Streptococcus pneumoniae surface thioredoxin-fold lipoproteins crucial for extracellular oxidative stress resistance and maintenance of virulence.
Saleh M, Bartual SG, Abdullah MR, Jensch I, Asmat TM, Petruschka L, Pribyl T, Gellert M, Lillig CH, Antelmann H, Hermoso JA, Hammerschmidt S
OpenAccess logo EMBO Mol Med 5 1852-70 (2013)
PMID: 24136784

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-101418 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Thioredoxin domain-containing protein Chain: A
Molecule details ›
Chain: A
Length: 190 amino acids
Theoretical weight: 21.17 KDa
Source organism: Streptococcus pneumoniae TIGR4
Expression system: Escherichia coli
UniProt:
  • Canonical: A0A0H2UP26 (Residues: 21-188; Coverage: 89%)
Gene name: SP_0659
Sequence domains: Redoxin
Structure domains: Glutaredoxin

Ligands and Environments

2 bound ligands:
Ligand GOL 5 x GOL
Ligand MG 9 x MG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-4
Spacegroup: P43212
Unit cell:
a: 62.85Å b: 62.85Å c: 89.6Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.183 0.182 0.197
Expression system: Escherichia coli

Quick links

Citations

16 review citations

Oxidative stress, protein damage and repair in bacteria.
Ezraty et al. (2017)
15 more

1 mention without citation

Molecular architecture of Streptococcus pneumoniae surface thioredoxin-fold lipoproteins crucial for extracellular oxidative stress resistance and maintenance of virulence.
Saleh et al. (2013)