› 2c79

X-ray diffraction
1.5Å resolution

The structure of a family 4 acetyl xylan esterase from Clostridium thermocellum in complex with a colbalt ion.

Released:
DOI: 10.2210/pdb2c79/pdb
PDB entry 2c79 coloured by chain, front view.
PDB entry 2c79 coloured by chain, side view.
PDB entry 2c79 coloured by chain, top view.
Source organism: Acetivibrio thermocellus
Primary publication:
Structure and activity of two metal ion-dependent acetylxylan esterases involved in plant cell wall degradation reveals a close similarity to peptidoglycan deacetylases.
Taylor EJ, Gloster TM, Turkenburg JP, Vincent F, Brzozowski AM, Dupont C, Shareck F, Centeno MS, Prates JA, Puchart V, Ferreira LM, Fontes CM, Biely P, Davies GJ
J Biol Chem 281 10968-75 (2006)
PMID: 16431911

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 domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-131485 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
endo-1,4-beta-xylanase Chain: A
Molecule details ›
Chain: A
Length: 216 amino acids
Theoretical weight: 23.93 KDa
Source organism: Acetivibrio thermocellus
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: O87119 (Residues: 477-683; Coverage: 30%)
Gene name: xynA
Sequence domains: Polysaccharide deacetylase
Structure domains: Glycoside hydrolase/deacetylase

Ligands and Environments

1 bound ligand:
Ligand CO 1 x CO
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-4
Spacegroup: P41212
Unit cell:
a: 105.775Å b: 105.775Å c: 35.349Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.132 0.13 0.172
Expression system: Escherichia coli BL21

Quick links

Citations

8 review citations

Structural variation in the glycan strands of bacterial peptidoglycan.
Vollmer W. (2008)
7 more

1 mention without citation

Structural and chemical biology of deacetylases for carbohydrates, proteins, small molecules and histones.
Bürger et al. (2018)