› 3ma0

X-ray diffraction
2.2Å resolution

Closed liganded crystal structure of xylose binding protein from Escherichia coli

Released:
DOI: 10.2210/pdb3ma0/pdb
PDB entry 3ma0 coloured by chain, front view.
PDB entry 3ma0 coloured by chain, side view.
PDB entry 3ma0 coloured by chain, top view.
Source organism: Escherichia coli str. K-12 substr. MG1655
Primary publication:
Conformational changes and ligand recognition of Escherichia coli D-xylose binding protein revealed.
Sooriyaarachchi S, Ubhayasekera W, Park C, Mowbray SL
J Mol Biol 402 657-68 (2010)
PMID: 20678502

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-153404 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
D-xylose-binding periplasmic protein Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 313 amino acids
Theoretical weight: 34.13 KDa
Source organism: Escherichia coli str. K-12 substr. MG1655
Expression system: Escherichia coli
UniProt:
  • Canonical: P37387 (Residues: 24-330; Coverage: 100%)
Gene names: JW3538, b3566, xylF, xylT
Sequence domains: Periplasmic binding protein domain
Structure domains: Rossmann fold

Ligands and Environments

1 bound ligand:
Ligand XYP 3 x XYP
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID29
Spacegroup: P3221
Unit cell:
a: 156.064Å b: 156.064Å c: 103.609Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.183 0.182 0.202
Expression system: Escherichia coli

Quick links

Citations

10 citation in other articles

A single-molecule dissection of ligand binding to a protein with intrinsic dynamics.
Kim et al. (2013)
9 more

3 mentions without citation

A xylose-stimulated xylanase-xylose binding protein chimera created by random nonhomologous recombination.
Ribeiro et al. (2016)
2 more