› 5lui

X-ray diffraction
1.5Å resolution

Structure of cutinase 1 from Thermobifida cellulosilytica

Released:
DOI: 10.2210/pdb5lui/pdb
PDB entry 5lui coloured by chain, front view.
PDB entry 5lui coloured by chain, side view.
PDB entry 5lui coloured by chain, top view.
Source organism: Thermobifida cellulosilytica
Primary publication:
Small cause, large effect: Structural characterization of cutinases from Thermobifida cellulosilytica.
Ribitsch D, Hromic A, Zitzenbacher S, Zartl B, Gamerith C, Pellis A, Jungbauer A, Łyskowski A, Steinkellner G, Gruber K, Tscheliessnig R, Herrero Acero E, Guebitz GM
Biotechnol Bioeng 114 2481-2488 (2017)
PMID: 28671263

Function and Biology Details

Reactions catalysed: 
(Ethylene terephthalate)(n) + H(2)O = (ethylene terephthalate)(n-1) + ethylene terephthalate
Cutin + H(2)O = cutin monomers
Biochemical function:
Biological process:
  • not assigned
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-123177 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Cutinase 1 Chain: A
Molecule details ›
Chain: A
Length: 265 amino acids
Theoretical weight: 28.65 KDa
Source organism: Thermobifida cellulosilytica
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: E9LVH8 (Residues: 1-262; Coverage: 100%)
Gene name: cut1
Sequence domains: Chlorophyllase
Structure domains: alpha/beta hydrolase

Ligands and Environments

3 bound ligands:
Ligand PEG 1 x PEG
Ligand MG 2 x MG
Ligand CL 3 x CL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PETRA III, DESY BEAMLINE P11
Spacegroup: C2
Unit cell:
a: 84.97Å b: 34.89Å c: 78.05Å
α: 90° β: 108.56° γ: 90°
R-values:
R R work R free
0.154 0.153 0.181
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

5 review citations

Surface engineering of polyester-degrading enzymes to improve efficiency and tune specificity.
Biundo et al. (2018)
4 more

11 mentions without citation

Current knowledge on enzymatic PET degradation and its possible application to waste stream management and other fields.
Kawai et al. (2019)
10 more