› 1gye

X-ray diffraction
2.5Å resolution

Structure of Cellvibrio cellulosa alpha-L-arabinanase complexed with Arabinohexaose

Released:
DOI: 10.2210/pdb1gye/pdb
PDB entry 1gye coloured by chain, front view.
PDB entry 1gye coloured by chain, side view.
PDB entry 1gye coloured by chain, top view.
Source organism: Cellvibrio japonicus
Primary publication:
Cellvibrio japonicus alpha-L-arabinanase 43A has a novel five-blade beta-propeller fold.
Nurizzo D, Turkenburg JP, Charnock SJ, Roberts SM, Dodson EJ, McKie VA, Taylor EJ, Gilbert HJ, Davies GJ
Nat Struct Biol 9 665-8 (2002)
PMID: 12198486

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:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-161157 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (2 distinct):
Extracellular exo-alpha-(1->5)-L-arabinofuranosidase ArbA Chain: B
Molecule details ›
Chain: B
Length: 315 amino acids
Theoretical weight: 35.85 KDa
Source organism: Cellvibrio japonicus
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P95470 (Residues: 32-346; Coverage: 100%)
Gene name: arbA
Sequence domains: Glycosyl hydrolases family 43
Structure domains: Glycosyl hydrolase domain; family 43

Ligands and Environments

Carbohydrate polymer : NEW Components: AHR
Carbohydrate polymer
1 bound ligand:
Ligand CL 1 x CL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-2
Spacegroup: P6522
Unit cell:
a: 90.605Å b: 90.605Å c: 177.554Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.19 0.188 0.238
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

13 review citations

Xylanases, xylanase families and extremophilic xylanases.
Collins et al. (2005)
12 more

4 mentions without citation

Crystal structure of an Exo-1,5-{alpha}-L-arabinofuranosidase from Streptomyces avermitilis provides insights into the mechanism of substrate discrimination between exo- and endo-type enzymes in glycoside hydrolase family 43.
Fujimoto et al. (2010)
3 more