› 1jt2

X-ray diffraction
1.8Å resolution

STRUCTURAL BASIS FOR THE SUBSTRATE SPECIFICITY OF THE FERUL DOMAIN OF THE CELLULOSOMAL XYLANASE Z FROM C. THERMOCELLUM

Released:
DOI: 10.2210/pdb1jt2/pdb
PDB entry 1jt2 coloured by chain, front view.
PDB entry 1jt2 coloured by chain, side view.
PDB entry 1jt2 coloured by chain, top view.
Source organism: Acetivibrio thermocellus
Primary publication:
Structural basis for the substrate specificity of the feruloyl esterase domain of the cellulosomal xylanase Z from Clostridium thermocellum.
Schubot FD, Kataeva IA, Blum DL, Shah AK, Ljungdahl LG, Rose JP, Wang BC
Biochemistry 40 12524-32 (2001)
PMID: 11601976

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-145316 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Endo-1,4-beta-xylanase Z Chain: A
Molecule details ›
Chain: A
Length: 268 amino acids
Theoretical weight: 29.05 KDa
Source organism: Acetivibrio thermocellus
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: P10478 (Residues: 20-287; Coverage: 32%)
Gene names: Cthe_1963, xynZ
Sequence domains: Putative esterase
Structure domains: alpha/beta hydrolase

Ligands and Environments

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

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU
Spacegroup: P6122
Unit cell:
a: 64.539Å b: 64.539Å c: 222.818Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.187 0.187 0.211
Expression system: Escherichia coli BL21

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Citations

7 review citations

Microbial hemicellulases.
Shallom et al. (2003)
6 more

6 mentions without citation

Degradation of complex arabinoxylans by human colonic Bacteroidetes.
Pereira et al. (2021)
5 more