› 2o6c

X-ray diffraction
1.7Å resolution

Structure of selenomethionyl rTp34 from Treponema pallidum

Released:
DOI: 10.2210/pdb2o6c/pdb
PDB entry 2o6c coloured by chain, front view.
PDB entry 2o6c coloured by chain, side view.
PDB entry 2o6c coloured by chain, top view.
Source organism: Treponema pallidum
Primary publication:
Crystal structure of the Tp34 (TP0971) lipoprotein of treponema pallidum: implications of its metal-bound state and affinity for human lactoferrin.
Deka RK, Brautigam CA, Tomson FL, Lumpkins SB, Tomchick DR, Machius M, Norgard MV
J Biol Chem 282 5944-58 (2007)
PMID: 17192261

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-148589 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
34 kDa membrane antigen Chains: A, B
Molecule details ›
Chains: A, B
Length: 189 amino acids
Theoretical weight: 20.72 KDa
Source organism: Treponema pallidum
Expression system: Escherichia coli
UniProt:
  • Canonical: P19478 (Residues: 16-204; Coverage: 100%)
Gene names: TP_0971, tpd
Sequence domains: Fe2+ transport protein
Structure domains: Periplasmic metal-binding protein Tp34-type

Ligands and Environments

3 bound ligands:
Ligand CL 4 x CL
Ligand EDO 2 x EDO
Ligand SO4 2 x SO4
1 modified residue:
Ligand MSE 12 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-ID
Spacegroup: P212121
Unit cell:
a: 34.41Å b: 66.02Å c: 150.992Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.187 0.184 0.215
Expression system: Escherichia coli

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Citations

8 review citations

Syphilis.
Peeling et al. (2017)
7 more