› 4g68

X-ray diffraction
1.8Å resolution

Biochemical and structural insights into xylan utilization by the thermophilic bacteriumcaldanaerobius polysaccharolyticus

Released:
DOI: 10.2210/pdb4g68/pdb
PDB entry 4g68 coloured by chain, front view.
PDB entry 4g68 coloured by chain, side view.
PDB entry 4g68 coloured by chain, top view.
Source organism: Caldanaerobius
Primary publication:
Biochemical and structural insights into xylan utilization by the thermophilic bacterium Caldanaerobius polysaccharolyticus.
Han Y, Agarwal V, Dodd D, Kim J, Bae B, Mackie RI, Nair SK, Cann IKO
J Biol Chem 287 34946-34960 (2012)
PMID: 22918832

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-125402 (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (4 distinct):
ABC transporter Chain: A
Molecule details ›
Chain: A
Length: 456 amino acids
Theoretical weight: 50.4 KDa
Source organism: Caldanaerobius
Expression system: Escherichia coli
UniProt:
  • Canonical: J9PBT4 (Residues: 1-442; Coverage: 100%)
Sequence domains: Bacterial extracellular solute-binding protein
Structure domains: Periplasmic binding protein-like II
ABC transporter Chain: B
Molecule details ›
Chain: B
Length: 432 amino acids
Theoretical weight: 47.87 KDa
Source organism: Caldanaerobius
Expression system: Escherichia coli
UniProt:
  • Canonical: J9PBT5 (Residues: 1-418; Coverage: 100%)
Sequence domains: Bacterial extracellular solute-binding protein
Structure domains: Periplasmic binding protein-like II
ABC transporter Chain: C
Molecule details ›
Chain: C
Length: 432 amino acids
Theoretical weight: 47.69 KDa
Source organism: Caldanaerobius
Expression system: Escherichia coli
UniProt:
  • Canonical: J9PBT5 (Residues: 1-418; Coverage: 100%)
Sequence domains: Bacterial extracellular solute-binding protein
Structure domains: Periplasmic binding protein-like II

Ligands and Environments

Carbohydrate polymer : NEW Components: XYS, XYP
Carbohydrate polymer
No bound ligands
1 modified residue:
Ligand MSE 12 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 21-ID-D
Spacegroup: P212121
Unit cell:
a: 59.33Å b: 150.862Å c: 150.879Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.231 0.23 0.26
Expression system: Escherichia coli

Quick links

Citations

6 review citations

Thermophiles in the genomic era: Biodiversity, science, and applications.
Urbieta et al. (2015)
5 more

5 mentions without citation

Molecular details of a starch utilization pathway in the human gut symbiont Eubacterium rectale.
Cockburn et al. (2015)
4 more