› 2yp6

X-ray diffraction
1.77Å resolution

Crystal structure of the pneumoccocal exposed lipoprotein thioredoxin sp_1000 (Etrx2) from Streptococcus pneumoniae strain TIGR4 in complex with Cyclofos 3 TM

Released:
DOI: 10.2210/pdb2yp6/pdb
PDB entry 2yp6 coloured by chain, front view.
PDB entry 2yp6 coloured by chain, side view.
PDB entry 2yp6 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
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-101433 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Thioredoxin domain-containing protein Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 185 amino acids
Theoretical weight: 20.72 KDa
Source organism: Streptococcus pneumoniae TIGR4
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: A0A0H2UPR5 (Residues: 1-185; Coverage: 100%)
Gene name: SP_1000
Sequence domains: Redoxin
Structure domains: Glutaredoxin

Ligands and Environments

2 bound ligands:
Ligand C6W 4 x C6W
Ligand MLI 8 x MLI
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-1
Spacegroup: P212121
Unit cell:
a: 61.46Å b: 116.31Å c: 116.42Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.166 0.165 0.19
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

15 review citations

Oxidative stress, protein damage and repair in bacteria.
Ezraty et al. (2017)
14 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)