› 2z79

X-ray diffraction
1.3Å resolution

High resolution crystal structure of a glycoside hydrolase family 11 xylanase of Bacillus subtilis

Released:
DOI: 10.2210/pdb2z79/pdb
PDB entry 2z79 coloured by chain, front view.
PDB entry 2z79 coloured by chain, side view.
PDB entry 2z79 coloured by chain, top view.
Source organism: Bacillus subtilis
Primary publication:
Crystallographic analysis shows substrate binding at the -3 to +1 active-site subsites and at the surface of glycoside hydrolase family 11 endo-1,4-beta-xylanases.
Vandermarliere E, Bourgois TM, Rombouts S, Van Campenhout S, Volckaert G, Strelkov SV, Delcour JA, Rabijns A, Courtin CM
Biochem J 410 71-9 (2008)
PMID: 17983355

Function and Biology Details

Reaction catalysed: 
Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-148365 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Endo-1,4-beta-xylanase A Chains: A, B
Molecule details ›
Chains: A, B
Length: 185 amino acids
Theoretical weight: 20.34 KDa
Source organism: Bacillus subtilis
Expression system: Escherichia coli
UniProt:
  • Canonical: P18429 (Residues: 29-213; Coverage: 100%)
Gene names: BSU18840, xynA
Sequence domains: Glycosyl hydrolases family 11
Structure domains: Jelly Rolls

Ligands and Environments

1 bound ligand:
Ligand GOL 8 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE BW7A
Spacegroup: P212121
Unit cell:
a: 40.87Å b: 63.059Å c: 122.435Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.158 0.157 0.176
Expression system: Escherichia coli

Quick links

Citations

3 review citations

Structural determinants of the substrate specificities of xylanases from different glycoside hydrolase families.
Pollet et al. (2010)
2 more

2 mentions without citation

Coupled chemistry kinetics demonstrate the utility of functionalized Sup35 amyloid nanofibrils in biocatalytic cascades.
Schmuck et al. (2019)
1 more