› 5vg0

X-ray diffraction
1.1Å resolution

Room temperature X-ray crystallographic structure of a Jonesia denitrificans lytic polysaccharide monooxygenase at 1.1 angstrom resolution.

Released:
DOI: 10.2210/pdb5vg0/pdb
PDB entry 5vg0 coloured by chain, front view.
PDB entry 5vg0 coloured by chain, side view.
PDB entry 5vg0 coloured by chain, top view.
Source organism: Jonesia denitrificans DSM 20603
Primary publication:
Neutron and Atomic Resolution X-ray Structures of a Lytic Polysaccharide Monooxygenase Reveal Copper-Mediated Dioxygen Binding and Evidence for N-Terminal Deprotonation.
Bacik JP, Mekasha S, Forsberg Z, Kovalevsky AY, Vaaje-Kolstad G, Eijsink VGH, Nix JC, Coates L, Cuneo MJ, Unkefer CJ, Chen JC
Biochemistry 56 2529-2532 (2017)
PMID: 28481095

Function and Biology Details

Reaction catalysed: 
Random endo-hydrolysis of N-acetyl-beta-D-glucosaminide (1->4)-beta-linkages in chitin and chitodextrins
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-111751 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
GH18 domain-containing protein Chains: A, B
Molecule details ›
Chains: A, B
Length: 142 amino acids
Theoretical weight: 15.54 KDa
Source organism: Jonesia denitrificans DSM 20603
Expression system: Escherichia coli
UniProt:
  • Canonical: C7R4I0 (Residues: 32-173; Coverage: 23%)
Gene name: Jden_1381
Sequence domains: Lytic polysaccharide mono-oxygenase, cellulose-degrading

Ligands and Environments

2 bound ligands:
Ligand CU 2 x CU
Ligand PER 2 x PER
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 4.2.2
Spacegroup: P212121
Unit cell:
a: 32.04Å b: 75.56Å c: 120.36Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.114 0.114 0.128
Expression system: Escherichia coli

Quick links

Citations

5 review citations

Oxidoreductases and Reactive Oxygen Species in Conversion of Lignocellulosic Biomass.
Bissaro et al. (2018)
4 more

4 mentions without citation

Mechanism of hydrogen peroxide formation by lytic polysaccharide monooxygenase.
Caldararu et al. (2019)
3 more