› 1vbu

X-ray diffraction
1.8Å resolution

Crystal structure of native xylanase 10B from Thermotoga maritima

Released:
DOI: 10.2210/pdb1vbu/pdb
PDB entry 1vbu coloured by chain, front view.
PDB entry 1vbu coloured by chain, side view.
PDB entry 1vbu coloured by chain, top view.
Source organism: Thermotoga maritima
Primary publication:
Structural basis of the substrate subsite and the highly thermal stability of xylanase 10B from Thermotoga maritima MSB8.
Kumasaka T, Kaneko T, Morokuma C, Yatsunami R, Sato T, Nakamura S, Tanaka N
Proteins 61 999-1009 (2005)
PMID: 16247799

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-194438 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Beta-xylanase Chains: A, B
Molecule details ›
Chains: A, B
Length: 328 amino acids
Theoretical weight: 38.7 KDa
Source organism: Thermotoga maritima
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9WXS5 (Residues: 20-347; Coverage: 95%)
Gene name: TM_0070
Sequence domains: Glycosyl hydrolase family 10
Structure domains: Glycosidases

Ligands and Environments

3 bound ligands:
Ligand SO4 1 x SO4
Ligand ACY 6 x ACY
Ligand GOL 2 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL38B1
Spacegroup: P1
Unit cell:
a: 58.5Å b: 59.1Å c: 61.34Å
α: 84.59° β: 71.14° γ: 68.32°
R-values:
R R work R free
0.191 0.186 0.218
Expression system: Escherichia coli

Quick links

Citations

2 review citations

Thermostable enzymes as biocatalysts in the biofuel industry.
Yeoman et al. (2010)
1 more

3 mentions without citation

Thermostability improvement of a streptomyces xylanase by introducing proline and glutamic acid residues.
Wang et al. (2014)
2 more