› 1zm1

X-ray diffraction
2.3Å resolution

Crystal structures of complex F. succinogenes 1,3-1,4-beta-D-glucanase and beta-1,3-1,4-cellotriose

Released:
DOI: 10.2210/pdb1zm1/pdb
PDB entry 1zm1 coloured by chain, front view.
PDB entry 1zm1 coloured by chain, side view.
PDB entry 1zm1 coloured by chain, top view.
Source organism: Fibrobacter succinogenes
Primary publication:
Crystal structure of truncated Fibrobacter succinogenes 1,3-1,4-beta-D-glucanase in complex with beta-1,3-1,4-cellotriose.
Tsai LC, Shyur LF, Cheng YS, Lee SH
J Mol Biol 354 642-51 (2005)
PMID: 16246371

Function and Biology Details

Reaction catalysed: 
Hydrolysis of (1->4)-beta-D-glucosidic linkages in beta-D-glucans containing (1->3)- and (1->4)-bonds
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-538796 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (2 distinct):
Beta-glucanase Chains: A, B
Molecule details ›
Chains: A, B
Length: 241 amino acids
Theoretical weight: 27.12 KDa
Source organism: Fibrobacter succinogenes
Expression system: Escherichia coli
UniProt:
  • Canonical: P17989 (Residues: 27-267; Coverage: 75%)
Gene names: FSU_0226, Fisuc_2961
Sequence domains: Glycosyl hydrolases family 16
Structure domains: Jelly Rolls

Ligands and Environments

Carbohydrate polymer : NEW Components: BGC
Carbohydrate polymer
1 bound ligand:
Ligand CA 2 x CA
1 modified residue:
Ligand MSE 8 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU300
Spacegroup: P21
Unit cell:
a: 70.148Å b: 43.97Å c: 81.015Å
α: 90° β: 109.56° γ: 90°
R-values:
R R work R free
0.18 0.18 0.264
Expression system: Escherichia coli

Quick links

Citations

13 citation in other articles

Diversity of glycosyl hydrolases from cellulose-depleting communities enriched from casts of two earthworm species.
Beloqui et al. (2010)
12 more

2 mentions without citation

The β-glucanase ZgLamA from Zobellia galactanivorans evolved a bent active site adapted for efficient degradation of algal laminarin.
Labourel et al. (2014)
1 more