› 6bgc

X-ray diffraction
2.08Å resolution

The crystal structure of the W145A variant of TpMglB-2 (Tp0684) with bound glucose

Released:
DOI: 10.2210/pdb6bgc/pdb
PDB entry 6bgc coloured by chain, front view.
PDB entry 6bgc coloured by chain, side view.
PDB entry 6bgc coloured by chain, top view.
Source organism: Treponema pallidum subsp. pallidum str. Nichols
Primary publication:
Crystal stuctures of MglB-2 (TP0684), a topologically variant d-glucose-binding protein from Treponema pallidum, reveal a ligand-induced conformational change.
Brautigam CA, Deka RK, Liu WZ, Norgard MV
Protein Sci 27 880-885 (2018)
PMID: 29318719

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-555126 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glucose/galactose-binding lipoprotein Chains: A, B
Molecule details ›
Chains: A, B
Length: 387 amino acids
Theoretical weight: 41.66 KDa
Source organism: Treponema pallidum subsp. pallidum str. Nichols
Expression system: Escherichia coli
UniProt:
  • Canonical: Q08255 (Residues: 36-403; Coverage: 97%)
Gene names: TP_0684, mglB, tpp38
Sequence domains:
Structure domains: Rossmann fold

Ligands and Environments

3 bound ligands:
Ligand BGC 2 x BGC
Ligand CA 2 x CA
Ligand EDO 2 x EDO
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-ID
Spacegroup: P1
Unit cell:
a: 42.257Å b: 61.592Å c: 70.35Å
α: 80.22° β: 77.58° γ: 72.72°
R-values:
R R work R free
0.182 0.18 0.22
Expression system: Escherichia coli

Quick links

Citations

3 citation in other articles

Using modern approaches to sedimentation velocity to detect conformational changes in proteins.
Brautigam et al. (2020)
2 more

2 mentions without citation

Stress-Responsive Periplasmic Chaperones in Bacteria.
Kim et al. (2021)
1 more