› 5mlt

X-ray diffraction
1.61Å resolution

Structural characterization of a carbohydrate substrate binding protein from Streptococcus pneumoniae

Released:
DOI: 10.2210/pdb5mlt/pdb
PDB entry 5mlt coloured by chain, front view.
PDB entry 5mlt coloured by chain, side view.
PDB entry 5mlt coloured by chain, top view.
Source organism: Streptococcus pneumoniae TIGR4
Primary publication:
Structural characterization of the Streptococcus pneumoniae carbohydrate substrate-binding protein SP0092.
Culurgioni S, Tang M, Walsh MA
Acta Crystallogr F Struct Biol Commun 73 54-61 (2017)
PMID: 28045395

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-101386 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Carbohydrate ABC transporter substrate-binding protein Chain: A
Molecule details ›
Chain: A
Length: 455 amino acids
Theoretical weight: 51.27 KDa
Source organism: Streptococcus pneumoniae TIGR4
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: A0A0H2UMY0 (Residues: 39-491; Coverage: 92%)
Gene name: SP_0092
Sequence domains:

Ligands and Environments

1 bound ligand:
Ligand ZN 3 x ZN
1 modified residue:
Ligand MSE 7 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I04
Spacegroup: C2
Unit cell:
a: 104.24Å b: 82.54Å c: 60.35Å
α: 90° β: 107.76° γ: 90°
R-values:
R R work R free
0.195 0.193 0.229
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

3 citation in other articles

ProX from marine Synechococcus spp. show a sole preference for glycine-betaine with differential affinity between ecotypes.
Ford et al. (2022)
2 more

1 mention without citation

Structural characterization of the Streptococcus pneumoniae carbohydrate substrate-binding protein SP0092.
Culurgioni et al. (2017)