› 3ug4

X-ray diffraction
2.15Å resolution

Crystal structure of alpha-L-arabinofuranosidase from Thermotoga maritima arabinose complex

Released:
DOI: 10.2210/pdb3ug4/pdb
PDB entry 3ug4 coloured by chain, front view.
PDB entry 3ug4 coloured by chain, side view.
PDB entry 3ug4 coloured by chain, top view.
Source organism: Thermotoga maritima
Primary publication:
Crystal structures of glycoside hydrolase family 51 α-L-arabinofuranosidase from Thermotoga maritima.
Im DH, Kimura K, Hayasaka F, Tanaka T, Noguchi M, Kobayashi A, Shoda S, Miyazaki K, Wakagi T, Fushinobu S
Biosci Biotechnol Biochem 76 423-8 (2012)
PMID: 22313787

Function and Biology Details

Reaction catalysed: 
Hydrolysis of terminal non-reducing alpha-L-arabinofuranoside residues in alpha-L-arabinosides
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo hexamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-194494 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
non-reducing end alpha-L-arabinofuranosidase Chains: A, B, C, D, E, F
Molecule details ›
Chains: A, B, C, D, E, F
Length: 504 amino acids
Theoretical weight: 57.41 KDa
Source organism: Thermotoga maritima
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9WYB7 (Residues: 1-484; Coverage: 100%)
Gene name: TM_0281
Sequence domains: Alpha-L-arabinofuranosidase C-terminal domain
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand TRS 11 x TRS
Ligand AHR 31 x AHR
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE BL-5A
Spacegroup: P21
Unit cell:
a: 100.483Å b: 160.639Å c: 154.841Å
α: 90° β: 92.44° γ: 90°
R-values:
R R work R free
0.169 0.167 0.207
Expression system: Escherichia coli

Quick links

Citations

2 review citations

β-xylosidases and α-L-arabinofuranosidases: accessory enzymes for arabinoxylan degradation.
Lagaert et al. (2014)
1 more

4 mentions without citation

CaBP1, a neuronal Ca2+ sensor protein, inhibits inositol trisphosphate receptors by clamping intersubunit interactions.
Li et al. (2013)
3 more