› 4ifz

X-ray diffraction
1.9Å resolution

Crystal structure of Treponema pallidum TP0796 Flavin trafficking protein, Mn(II)-AMP product bound form

Released:
DOI: 10.2210/pdb4ifz/pdb
PDB entry 4ifz coloured by chain, front view.
PDB entry 4ifz coloured by chain, side view.
PDB entry 4ifz coloured by chain, top view.
Source organism: Treponema pallidum subsp. pallidum str. Nichols
Primary publication:
The TP0796 lipoprotein of Treponema pallidum is a bimetal-dependent FAD pyrophosphatase with a potential role in flavin homeostasis.
Deka RK, Brautigam CA, Liu WZ, Tomchick DR, Norgard MV
J Biol Chem 288 11106-21 (2013)
PMID: 23447540

Function and Biology Details

Reaction catalysed: 
FAD + [protein]-L-threonine = [protein]-FMN-L-threonine + AMP
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-131391 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
FAD:protein FMN transferase Chain: A
Molecule details ›
Chain: A
Length: 340 amino acids
Theoretical weight: 36.74 KDa
Source organism: Treponema pallidum subsp. pallidum str. Nichols
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: O83774 (Residues: 23-362; Coverage: 100%)
Gene names: TP_0796, apbE
Sequence domains: ApbE family
Structure domains: ApbE-like domains

Ligands and Environments

3 bound ligands:
Ligand AMP 1 x AMP
Ligand MG 1 x MG
Ligand MN 1 x MN
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-ID
Spacegroup: C2
Unit cell:
a: 116.632Å b: 46.907Å c: 57.625Å
α: 90° β: 102.17° γ: 90°
R-values:
R R work R free
0.161 0.158 0.203
Expression system: Escherichia coli BL21(DE3)

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Citations

3 review citations

Treponema pallidum, the syphilis spirochete: making a living as a stealth pathogen.
Radolf et al. (2016)
2 more

1 mention without citation

The TP0796 lipoprotein of Treponema pallidum is a bimetal-dependent FAD pyrophosphatase with a potential role in flavin homeostasis.
Deka et al. (2013)