› 2vpn

X-ray diffraction
1.55Å resolution

High-resolution structure of the periplasmic ectoine-binding protein from TeaABC TRAP-transporter of Halomonas elongata

Released:
DOI: 10.2210/pdb2vpn/pdb
PDB entry 2vpn coloured by chain, front view.
PDB entry 2vpn coloured by chain, side view.
PDB entry 2vpn coloured by chain, top view.
Source organism: Halomonas elongata
Primary publication:
1.55 A structure of the ectoine binding protein TeaA of the osmoregulated TRAP-transporter TeaABC from Halomonas elongata.
Kuhlmann SI, Terwisscha van Scheltinga AC, Bienert R, Kunte HJ, Ziegler C
Biochemistry 47 9475-85 (2008)
PMID: 18702523

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-122801 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Ectoine-binding periplasmic protein TeaA Chains: A, B
Molecule details ›
Chains: A, B
Length: 316 amino acids
Theoretical weight: 35.71 KDa
Source organism: Halomonas elongata
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: E1VBK1 (Residues: 26-341; Coverage: 100%)
Gene names: HELO_4274, teaA
Sequence domains: Bacterial extracellular solute-binding protein, family 7
Structure domains: Bacterial extracellular solute-binding protein, family 7

Ligands and Environments

2 bound ligands:
Ligand 4CS 2 x 4CS
Ligand MG 8 x MG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X10SA
Spacegroup: P1
Unit cell:
a: 48.3Å b: 52.2Å c: 63.5Å
α: 80.8° β: 85.8° γ: 77.9°
R-values:
R R work R free
0.159 0.158 0.204
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

4 review citations

Tripartite ATP-independent periplasmic (TRAP) transporters in bacteria and archaea.
Mulligan et al. (2011)
3 more

7 mentions without citation

Role of the Extremolytes Ectoine and Hydroxyectoine as Stress Protectants and Nutrients: Genetics, Phylogenomics, Biochemistry, and Structural Analysis.
Czech et al. (2018)
6 more